Polypeptides,peptides, types of peptides, structure of dipeptide, tripeptide and oligopeptide and different functions of peptide
•Download as PPTX, PDF•
1 like•1,244 views
Descriptive notes on polypeptides Polypeptides,peptides, types of peptides, structure of dipeptide, tripeptide and oligopeptide and different functions of peptide
Report
Share
Report
Share
Recommended
Peptides
Peptides are short chains of amino acids linked by peptide bonds. They are distinguished from proteins by typically containing fewer than 50 amino acid units. Peptides are formed through condensation reactions between carboxyl and amino groups of separate amino acids, releasing a water molecule. Peptide bonds are rigid and planar, contributing to protein structure stability. Peptides serve many important biological functions and can be classified based on their production method, including through ribosomal translation, nonribosomal synthesis, and enzymatic digestion of proteins in foods. Bioactive peptides derived from food proteins can have beneficial effects like lowering blood pressure, cholesterol, and antimicrobial properties.
Peptides and proteins structure and functions
Peptides and proteins are polymers of amino acids. Their structure and function depend on the nature, sequence, and spatial arrangement of amino acids. Peptides generally have fewer than 100 amino acids, while proteins have 100 or more. Many peptides are formed by protein breakdown. Examples of physiologically active peptides include glutathione, bradykinin, angiotensin, vasopressin, oxytocin, and TRH. Proteins perform functions like maintaining pH and osmotic balance. They also include enzymes, hormones, and structural components of tissues.
Protein chemistry P1 by Dr. Anurag Yadav
This document provides an overview of protein chemistry and amino acids. It defines amino acids as organic compounds containing amino and carboxyl groups. Amino acids combine via peptide bonds to form proteins. There are 20 standard amino acids that make up human proteins. Amino acids are classified based on structure, side chains, and metabolic fate. They have various physical and chemical properties important for protein structure and function. Amino acid derivatives also have biological significance as neurotransmitters, hormones, and drugs.
Bpt 114. purine and pyrimidine metabolism
Purines and pyrimidines are heterocyclic nitrogen-containing compounds that are major components of nucleotides, which build DNA and RNA. They function as building blocks of nucleic acids and are involved in various cellular processes as components of coenzymes and metabolic regulators. Nucleotides are synthesized through both de novo and salvage pathways. The de novo synthesis of purines involves multiple steps utilizing various substrates and is regulated at several points to control nucleotide levels. IMP is an early intermediate that is converted to AMP and GMP through reciprocal regulation. Purine degradation yields uric acid, while ingested nucleic acids undergo digestion and absorption as nucleosides and bases to contribute to nucleotide synthesis.
Lipids Ppt.
1. LIPIDS.
2. PROPERTIES OF LIPIDS.
3. FATTY ACIDS.
4. USES AND CLASSIFICATION OF FATTY ACIDS.
5. STRUCTURE AND CLASSIFICATION OF LIPIDS.
PHOSPHOLIPIDS: A class of lipid that is a key component of all cell membranes, as they can form lipid biomarkers. Composition: It is composed of phospholipids. i. Glycerol: one molecule ii. Fatty acids: Two molecules. iii. Phosphoric acid: one molecule. When a nitrogen-containing phospholipid group is attached to the end of the phospholipid, it is called phosphatidylcholine. Phospholipids consist of two parts i) Chapter: The head is polar in nature, soluble in water (hydrophilic). n) Tails: Nature has a non-polar tail, insoluble in water (hydrophobic).
Washes: Wax lipids are derived. Wax is a fatty acid ester and chronic alcohol: The wax is composed of i) a long-chain fatty acid ... one molecules ii) long-chain alcohol with one hydroxyl group (-OH), i.e. Cylinder wax is hydrophobic in nature. They have a high melting point, solid at room temperature. it gives stability and declines. On the surfaces of parts of plants, e.g. The leaves and fruits produce a waterproof layer, reducing the rate of perspiration. Wax is also a layer of wax that covers the bodies of animals, e.g., slime, insects, etc.
STEROIDS: Steroids fall under the lipid categories: Steroids are derived from lipid composition: proper arrangement of 3 cyclohexyl rings and 1 cyclopentane ring, a total of 17 carbon atoms in four carbon rings. Steroids do not contain alcohol and fatty acids.
Steroids Examples of steroids: i) Cholesterol: an important factor in animal cells. The precursor of all hormonal molecules such as aldosterone, sex hormone, and vitamin D ii) Aldosterone helps regulate Na+ions in the blood iii) Sex hormones e.g. testosterone, progesterone, and estrogens help to preserve the characteristics of males and females.
TERPENOIDES: It contains a very different class of organic compounds. Terpenoids are lipid derivatives, soluble in fat and soluble in water. Don't use molecule acids like fats. Composite units which they call isoprenoid or isoprenes. Isoprene unit: Hydrocarbon containing five carbon atoms with a branched-chain structure. Isoprene units bind to each other through the condensation process resulting in different types of compounds, e.g. Carotenoids, terpenes, and rubbers, etc.
CAROTENOIDS: Carotenoids are yellow, orange, red, or brown in plants. There are two kinds: i) Carotene: ii) Xanthophylla, i) Carotene: Orange is the genus of carotene, with red color, beta carotene. carrot & rice. Breakdown of beta-carotene leaves two molecules of vitamin A in the human body. n) Xanthophyllus: the auxiliary yellow color found in plants.
6 STORAGE LIPIDS.
7. USES OF LIPIDS.
# ALL ABOUT LIPIDS BY AUTHENTIC BOOKS.
Amino acid structure classification and properties
This document discusses the structure, classification, and properties of amino acids. It begins by defining amino acids as the building blocks of proteins. It then covers amino acid structure, various classification systems including based on polarity and R groups, and essential vs. non-essential amino acids. The document also discusses the physical, chemical, and biological properties of specific amino acids like alanine, valine, leucine, and others. It provides information on isoelectric points and gives examples of biochemical tests used to identify different amino acids.
Protein structure
- Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure is the 3D shape formed by interactions between different parts of the polypeptide. Quaternary structure refers to the assembly of multiple polypeptide subunits.
Regulation of fattyacid metabolism
Fatty acid metabolism is regulated through acetyl-CoA carboxylase, which catalyzes the committed step of fatty acid biosynthesis. Acetyl-CoA carboxylase activity is controlled by hormones like insulin, glucagon, and epinephrine in response to energy levels. Insulin stimulates fatty acid synthesis by activating acetyl-CoA carboxylase through dephosphorylation. Glucagon and epinephrine inhibit fatty acid synthesis by phosphorylating and inactivating acetyl-CoA carboxylase. Fatty acid oxidation is regulated by fatty acid levels and is stimulated by hormones like glucagon and epinephrine through lipolysis and phosphorylation of enzymes.
Recommended
Peptides
Peptides are short chains of amino acids linked by peptide bonds. They are distinguished from proteins by typically containing fewer than 50 amino acid units. Peptides are formed through condensation reactions between carboxyl and amino groups of separate amino acids, releasing a water molecule. Peptide bonds are rigid and planar, contributing to protein structure stability. Peptides serve many important biological functions and can be classified based on their production method, including through ribosomal translation, nonribosomal synthesis, and enzymatic digestion of proteins in foods. Bioactive peptides derived from food proteins can have beneficial effects like lowering blood pressure, cholesterol, and antimicrobial properties.
Peptides and proteins structure and functions
Peptides and proteins are polymers of amino acids. Their structure and function depend on the nature, sequence, and spatial arrangement of amino acids. Peptides generally have fewer than 100 amino acids, while proteins have 100 or more. Many peptides are formed by protein breakdown. Examples of physiologically active peptides include glutathione, bradykinin, angiotensin, vasopressin, oxytocin, and TRH. Proteins perform functions like maintaining pH and osmotic balance. They also include enzymes, hormones, and structural components of tissues.
Protein chemistry P1 by Dr. Anurag Yadav
This document provides an overview of protein chemistry and amino acids. It defines amino acids as organic compounds containing amino and carboxyl groups. Amino acids combine via peptide bonds to form proteins. There are 20 standard amino acids that make up human proteins. Amino acids are classified based on structure, side chains, and metabolic fate. They have various physical and chemical properties important for protein structure and function. Amino acid derivatives also have biological significance as neurotransmitters, hormones, and drugs.
Bpt 114. purine and pyrimidine metabolism
Purines and pyrimidines are heterocyclic nitrogen-containing compounds that are major components of nucleotides, which build DNA and RNA. They function as building blocks of nucleic acids and are involved in various cellular processes as components of coenzymes and metabolic regulators. Nucleotides are synthesized through both de novo and salvage pathways. The de novo synthesis of purines involves multiple steps utilizing various substrates and is regulated at several points to control nucleotide levels. IMP is an early intermediate that is converted to AMP and GMP through reciprocal regulation. Purine degradation yields uric acid, while ingested nucleic acids undergo digestion and absorption as nucleosides and bases to contribute to nucleotide synthesis.
Lipids Ppt.
1. LIPIDS.
2. PROPERTIES OF LIPIDS.
3. FATTY ACIDS.
4. USES AND CLASSIFICATION OF FATTY ACIDS.
5. STRUCTURE AND CLASSIFICATION OF LIPIDS.
PHOSPHOLIPIDS: A class of lipid that is a key component of all cell membranes, as they can form lipid biomarkers. Composition: It is composed of phospholipids. i. Glycerol: one molecule ii. Fatty acids: Two molecules. iii. Phosphoric acid: one molecule. When a nitrogen-containing phospholipid group is attached to the end of the phospholipid, it is called phosphatidylcholine. Phospholipids consist of two parts i) Chapter: The head is polar in nature, soluble in water (hydrophilic). n) Tails: Nature has a non-polar tail, insoluble in water (hydrophobic).
Washes: Wax lipids are derived. Wax is a fatty acid ester and chronic alcohol: The wax is composed of i) a long-chain fatty acid ... one molecules ii) long-chain alcohol with one hydroxyl group (-OH), i.e. Cylinder wax is hydrophobic in nature. They have a high melting point, solid at room temperature. it gives stability and declines. On the surfaces of parts of plants, e.g. The leaves and fruits produce a waterproof layer, reducing the rate of perspiration. Wax is also a layer of wax that covers the bodies of animals, e.g., slime, insects, etc.
STEROIDS: Steroids fall under the lipid categories: Steroids are derived from lipid composition: proper arrangement of 3 cyclohexyl rings and 1 cyclopentane ring, a total of 17 carbon atoms in four carbon rings. Steroids do not contain alcohol and fatty acids.
Steroids Examples of steroids: i) Cholesterol: an important factor in animal cells. The precursor of all hormonal molecules such as aldosterone, sex hormone, and vitamin D ii) Aldosterone helps regulate Na+ions in the blood iii) Sex hormones e.g. testosterone, progesterone, and estrogens help to preserve the characteristics of males and females.
TERPENOIDES: It contains a very different class of organic compounds. Terpenoids are lipid derivatives, soluble in fat and soluble in water. Don't use molecule acids like fats. Composite units which they call isoprenoid or isoprenes. Isoprene unit: Hydrocarbon containing five carbon atoms with a branched-chain structure. Isoprene units bind to each other through the condensation process resulting in different types of compounds, e.g. Carotenoids, terpenes, and rubbers, etc.
CAROTENOIDS: Carotenoids are yellow, orange, red, or brown in plants. There are two kinds: i) Carotene: ii) Xanthophylla, i) Carotene: Orange is the genus of carotene, with red color, beta carotene. carrot & rice. Breakdown of beta-carotene leaves two molecules of vitamin A in the human body. n) Xanthophyllus: the auxiliary yellow color found in plants.
6 STORAGE LIPIDS.
7. USES OF LIPIDS.
# ALL ABOUT LIPIDS BY AUTHENTIC BOOKS.
Amino acid structure classification and properties
This document discusses the structure, classification, and properties of amino acids. It begins by defining amino acids as the building blocks of proteins. It then covers amino acid structure, various classification systems including based on polarity and R groups, and essential vs. non-essential amino acids. The document also discusses the physical, chemical, and biological properties of specific amino acids like alanine, valine, leucine, and others. It provides information on isoelectric points and gives examples of biochemical tests used to identify different amino acids.
Protein structure
- Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure is the 3D shape formed by interactions between different parts of the polypeptide. Quaternary structure refers to the assembly of multiple polypeptide subunits.
Regulation of fattyacid metabolism
Fatty acid metabolism is regulated through acetyl-CoA carboxylase, which catalyzes the committed step of fatty acid biosynthesis. Acetyl-CoA carboxylase activity is controlled by hormones like insulin, glucagon, and epinephrine in response to energy levels. Insulin stimulates fatty acid synthesis by activating acetyl-CoA carboxylase through dephosphorylation. Glucagon and epinephrine inhibit fatty acid synthesis by phosphorylating and inactivating acetyl-CoA carboxylase. Fatty acid oxidation is regulated by fatty acid levels and is stimulated by hormones like glucagon and epinephrine through lipolysis and phosphorylation of enzymes.
Protein structure: details
This document discusses the different levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure refers to the amino acid sequence. Secondary structure includes alpha helices, beta sheets, and beta turns formed by hydrogen bonding between amino acids. Tertiary structure is the 3D conformation determined by interactions between side chains. Quaternary structure refers to the arrangement of multiple polypeptide subunits in multimeric proteins. The structures are determined through techniques like X-ray crystallography and NMR.
Amino acid
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They perform important functions including serving as monomers for protein synthesis, participating in cellular processes, and acting as precursors for other compounds.
Amino acid -Classification of amino acid, Properties, peptides-Types and bio...
This document provides an overview of amino acids and peptides. It defines amino acids as organic compounds containing amino and carboxyl groups that serve as the building blocks of proteins. The document classifies amino acids based on their structure, polarity, metabolic rates, and nutritional properties. It also discusses the general structure of amino acids, their physical and chemical properties, functions, and roles as drugs. The document defines peptides as compounds formed via amide linkages between amino acids, and describes different types of peptides and their functions, including as precursors to proteins, hormones, structural components, and more.
Chemistry of amino acids
Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up proteins. Amino acids have a general structure that includes an amino group, a carboxyl group, and a side chain. They can be classified based on their structure, side chain properties, nutritional requirements, and metabolic fate. Common properties of amino acids include being crystalline solids, existing as zwitterions with an isoelectric point, and having chirality with L and D isomers. Amino acids undergo various reactions due to their amino, carboxyl, and side chain groups.
PROTEINS
Proteins have a variety of important functions in living organisms. They are made up of chains of amino acids that join together to form complex structures ranging from simple primary to advanced quaternary structures which determine their specific roles. Globular proteins have spherical shapes defined by their amino acid sequences which allow metabolic functions like enzymatic reactions, while changes in structure through denaturation disrupt protein functioning.
Lipids
Lipids have a hydrophobic nature due to hydrocarbon chains. They are insoluble in water but soluble in nonpolar solvents. Major lipids include fatty acids, triacylglycerols, phospholipids, cholesterol, and steroid hormones. Fatty acids are used for energy storage and membrane components. Triacylglycerols store fatty acids as an energy source. Phospholipids are major membrane components. Cholesterol is important for membrane structure and steroid hormone synthesis. Lipids are digested into fatty acids and monoacylglycerols then absorbed into intestinal cells to form chylomicrons which transport lipids through lymph and blood.
Lipids
This document summarizes key information about lipids and fats:
1. Lipids are organic compounds that are greasy to touch and insoluble in water but soluble in organic solvents. They contain carbon, hydrogen, oxygen, nitrogen and phosphorus and are a concentrated source of energy.
2. Fats are composed of triglycerides, which are esters of glycerol and fatty acids. Fatty acids are the building blocks of several lipid classes. Unsaturated fatty acids contain one or more double bonds and are important for growth and health.
3. Lipids serve many functions in the body including as an energy source, insulating and protecting tissues, carrying fat-soluble vitamins, and
Complex Lipids (Phosholipids, Glycolipids and Lipoproteins) (Chemistry of Lip...
This document discusses different types of phospholipids and their structures and functions. It notes that phospholipids are made up of fatty acids, glycerol, phosphoric acid, and a nitrogenous base. They are major constituents of cell membranes and are amphipathic in nature. The document describes different classes of phospholipids, including phosphatidylcholines, phosphatidylethanolamines, phosphatidylserines, cardiolipins, sphingomyelins, and phosphatidylinositols. It also discusses glycolipids and lipoproteins, providing details on their compositions and roles in cells and tissues.
Amino acids and Protein chemistry by Dr. Anurag Yadav
Amino acid chemistry
Protein chemistry
Amino acid & Protein structure, organisation, properties and classification
for MBBS, BDS, MSc, BSc, BPT, Nursing
Youtube: https://youtu.be/CP_PL21mqOc
Proteins
Fish proteins are an important source of nutrition in the Philippines. Proteins are composed of amino acids, with 20 standard amino acids serving as the building blocks. When cells make proteins, amino acid groups are linked together to form polypeptide chains of varying lengths. A protein's structure can be primary, secondary, tertiary, or quaternary depending on interactions between amino acid chains. Proteins are classified by their composition as simple proteins like albumins and globulins, or conjugated proteins which contain additional groups. They are also classified by function, with examples being structural, contractile, enzymatic, hormonal, and blood proteins. Protein breakdown through autolysis leads to changes in fish flesh quality over time.
Nucleotides metabolism
This document discusses nucleotides, their synthesis and degradation. It covers the following key points:
1. Nucleotides are composed of a nucleoside (a nitrogenous base linked to a 5-carbon sugar) bound to one or more phosphate groups. They are the monomers that make up nucleic acids like RNA and DNA.
2. Purine nucleotides are synthesized de novo through a complex 10 step pathway beginning with phosphoribosyl pyrophosphate (PRPP) and ending with inosine monophosphate (IMP). Pyrimidine nucleotides can also be synthesized from PRPP.
3. Nucleotides can be broken down through both intracellular catabolism pathways that generate purine
Protein structure
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
PROTEINS
This document discusses proteins, including their definition, composition, sources, storage, requirements, functions, structure, and classification. Some key points:
- Proteins are polypeptides composed of amino acids joined by peptide bonds. They are essential to life and perform many catalytic, structural, transport, and other functions.
- Sources of proteins include animal sources like meat and dairy as well as plant sources like legumes. Storage capacity in organisms is limited compared to carbohydrates and fats.
- Proteins are classified based on their nutritional value, function, structure, and physicochemical properties. Complete proteins contain all essential amino acids while incomplete proteins lack some.
- Structure depends on shape - globular
Biomolecules
I have prepare this slide thinking that it will help students .I have collected different photos and videos from internet please comment and if you need any slides for a topics . i will prepare the slide .
Amino acid
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a specific side chain. They are classified as essential, non-essential, or conditional depending on whether the human body can synthesize them. Amino acids are the building blocks of proteins and participate in many important biological functions and cellular processes. They have various physical and chemical properties depending on their specific structure and side chain, and many amino acids have medicinal properties and play roles in treating diseases.
Peptide bond
Peptide bonds form during translation within ribosomes and connect amino acids into polypeptide chains that fold into protein structures. A peptide bond is a covalent bond formed through a dehydration synthesis reaction between the carboxyl group of one amino acid and the amine group of the next. This reaction involves the loss of a water molecule as the carboxyl oxygen and amine hydrogen are removed to connect the amino acids. Peptide bonds make up the backbone of proteins by linking the 20 common amino acids together end to end.
Enzymes
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They achieve high reaction rates through substrate binding and shape complementarity. Enzyme activity is affected by factors like temperature, pH, and salt concentration that can alter protein structure. Most enzymes exhibit high specificity for their substrate. Inhibition studies provide information about enzyme mechanisms and active sites. Regulation of enzyme activity occurs through feedback inhibition, allosteric regulation, covalent modification like phosphorylation, and conversion of inactive zymogens to active forms.
Chemical synthesis of polypetide presentation (1)
biomedical potential of polypeptide. its synthesis, schematic flow of solid phase peptide synthesis.
Chemistry of amino acids
The document provides information about amino acids and their classification. It discusses that amino acids are the monomer units that make up protein polymers. They can be classified based on their structure, side chains, nutritional requirements, and metabolic fate. The 20 standard amino acids are discussed in detail, including their physical and chemical properties. Key reactions of amino acids involving their amino, carboxyl, and side chain groups are also summarized.
Lipid200 structure and function
Lipids are a diverse group of compounds that are insoluble in water but soluble in organic solvents. They include fats, oils, waxes, sterols, and phospholipids. The document discusses the structure, function, and classification of various lipids. It describes simple lipids like triglycerides and waxes, as well as complex lipids including phospholipids. Phospholipids are important structural components of cell membranes and contain a phosphate group, alcohol, and fatty acids. Glycerophospholipids are the major class of phospholipids, with phosphatidylcholine, phosphatidylethanolamine, and others playing important roles in cells and tissues.
Peptide by KK Sahu sir
Introduction
Definition
Structure of peptide bond
Classes
Dipeptides
Tripeptides
Polypeptides
Peptide synthesis
Liquid phase synthesis
Solid phase synthesis
General principle
Steps
Peptide overview
Application
Conclusion
References
peptides proteins ppt
Peptides and proteins are composed of chains of amino acids linked by peptide bonds. Peptides contain 2-50 amino acids while proteins have 50 or more. The primary structure of a peptide or protein refers to the specific sequence of amino acids. This sequence can be determined through amino acid composition analysis and methods like terminal residue analysis and partial hydrolysis, which selectively label and remove amino acids from the termini to reveal the sequence one by one. Determining the primary structure is important as changes in just one amino acid can impact structure and function.
More Related Content
What's hot
Protein structure: details
This document discusses the different levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure refers to the amino acid sequence. Secondary structure includes alpha helices, beta sheets, and beta turns formed by hydrogen bonding between amino acids. Tertiary structure is the 3D conformation determined by interactions between side chains. Quaternary structure refers to the arrangement of multiple polypeptide subunits in multimeric proteins. The structures are determined through techniques like X-ray crystallography and NMR.
Amino acid
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They perform important functions including serving as monomers for protein synthesis, participating in cellular processes, and acting as precursors for other compounds.
Amino acid -Classification of amino acid, Properties, peptides-Types and bio...
This document provides an overview of amino acids and peptides. It defines amino acids as organic compounds containing amino and carboxyl groups that serve as the building blocks of proteins. The document classifies amino acids based on their structure, polarity, metabolic rates, and nutritional properties. It also discusses the general structure of amino acids, their physical and chemical properties, functions, and roles as drugs. The document defines peptides as compounds formed via amide linkages between amino acids, and describes different types of peptides and their functions, including as precursors to proteins, hormones, structural components, and more.
Chemistry of amino acids
Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up proteins. Amino acids have a general structure that includes an amino group, a carboxyl group, and a side chain. They can be classified based on their structure, side chain properties, nutritional requirements, and metabolic fate. Common properties of amino acids include being crystalline solids, existing as zwitterions with an isoelectric point, and having chirality with L and D isomers. Amino acids undergo various reactions due to their amino, carboxyl, and side chain groups.
PROTEINS
Proteins have a variety of important functions in living organisms. They are made up of chains of amino acids that join together to form complex structures ranging from simple primary to advanced quaternary structures which determine their specific roles. Globular proteins have spherical shapes defined by their amino acid sequences which allow metabolic functions like enzymatic reactions, while changes in structure through denaturation disrupt protein functioning.
Lipids
Lipids have a hydrophobic nature due to hydrocarbon chains. They are insoluble in water but soluble in nonpolar solvents. Major lipids include fatty acids, triacylglycerols, phospholipids, cholesterol, and steroid hormones. Fatty acids are used for energy storage and membrane components. Triacylglycerols store fatty acids as an energy source. Phospholipids are major membrane components. Cholesterol is important for membrane structure and steroid hormone synthesis. Lipids are digested into fatty acids and monoacylglycerols then absorbed into intestinal cells to form chylomicrons which transport lipids through lymph and blood.
Lipids
This document summarizes key information about lipids and fats:
1. Lipids are organic compounds that are greasy to touch and insoluble in water but soluble in organic solvents. They contain carbon, hydrogen, oxygen, nitrogen and phosphorus and are a concentrated source of energy.
2. Fats are composed of triglycerides, which are esters of glycerol and fatty acids. Fatty acids are the building blocks of several lipid classes. Unsaturated fatty acids contain one or more double bonds and are important for growth and health.
3. Lipids serve many functions in the body including as an energy source, insulating and protecting tissues, carrying fat-soluble vitamins, and
Complex Lipids (Phosholipids, Glycolipids and Lipoproteins) (Chemistry of Lip...
This document discusses different types of phospholipids and their structures and functions. It notes that phospholipids are made up of fatty acids, glycerol, phosphoric acid, and a nitrogenous base. They are major constituents of cell membranes and are amphipathic in nature. The document describes different classes of phospholipids, including phosphatidylcholines, phosphatidylethanolamines, phosphatidylserines, cardiolipins, sphingomyelins, and phosphatidylinositols. It also discusses glycolipids and lipoproteins, providing details on their compositions and roles in cells and tissues.
Amino acids and Protein chemistry by Dr. Anurag Yadav
Amino acid chemistry
Protein chemistry
Amino acid & Protein structure, organisation, properties and classification
for MBBS, BDS, MSc, BSc, BPT, Nursing
Youtube: https://youtu.be/CP_PL21mqOc
Proteins
Fish proteins are an important source of nutrition in the Philippines. Proteins are composed of amino acids, with 20 standard amino acids serving as the building blocks. When cells make proteins, amino acid groups are linked together to form polypeptide chains of varying lengths. A protein's structure can be primary, secondary, tertiary, or quaternary depending on interactions between amino acid chains. Proteins are classified by their composition as simple proteins like albumins and globulins, or conjugated proteins which contain additional groups. They are also classified by function, with examples being structural, contractile, enzymatic, hormonal, and blood proteins. Protein breakdown through autolysis leads to changes in fish flesh quality over time.
Nucleotides metabolism
This document discusses nucleotides, their synthesis and degradation. It covers the following key points:
1. Nucleotides are composed of a nucleoside (a nitrogenous base linked to a 5-carbon sugar) bound to one or more phosphate groups. They are the monomers that make up nucleic acids like RNA and DNA.
2. Purine nucleotides are synthesized de novo through a complex 10 step pathway beginning with phosphoribosyl pyrophosphate (PRPP) and ending with inosine monophosphate (IMP). Pyrimidine nucleotides can also be synthesized from PRPP.
3. Nucleotides can be broken down through both intracellular catabolism pathways that generate purine
Protein structure
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
PROTEINS
This document discusses proteins, including their definition, composition, sources, storage, requirements, functions, structure, and classification. Some key points:
- Proteins are polypeptides composed of amino acids joined by peptide bonds. They are essential to life and perform many catalytic, structural, transport, and other functions.
- Sources of proteins include animal sources like meat and dairy as well as plant sources like legumes. Storage capacity in organisms is limited compared to carbohydrates and fats.
- Proteins are classified based on their nutritional value, function, structure, and physicochemical properties. Complete proteins contain all essential amino acids while incomplete proteins lack some.
- Structure depends on shape - globular
Biomolecules
I have prepare this slide thinking that it will help students .I have collected different photos and videos from internet please comment and if you need any slides for a topics . i will prepare the slide .
Amino acid
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a specific side chain. They are classified as essential, non-essential, or conditional depending on whether the human body can synthesize them. Amino acids are the building blocks of proteins and participate in many important biological functions and cellular processes. They have various physical and chemical properties depending on their specific structure and side chain, and many amino acids have medicinal properties and play roles in treating diseases.
Peptide bond
Peptide bonds form during translation within ribosomes and connect amino acids into polypeptide chains that fold into protein structures. A peptide bond is a covalent bond formed through a dehydration synthesis reaction between the carboxyl group of one amino acid and the amine group of the next. This reaction involves the loss of a water molecule as the carboxyl oxygen and amine hydrogen are removed to connect the amino acids. Peptide bonds make up the backbone of proteins by linking the 20 common amino acids together end to end.
Enzymes
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They achieve high reaction rates through substrate binding and shape complementarity. Enzyme activity is affected by factors like temperature, pH, and salt concentration that can alter protein structure. Most enzymes exhibit high specificity for their substrate. Inhibition studies provide information about enzyme mechanisms and active sites. Regulation of enzyme activity occurs through feedback inhibition, allosteric regulation, covalent modification like phosphorylation, and conversion of inactive zymogens to active forms.
Chemical synthesis of polypetide presentation (1)
biomedical potential of polypeptide. its synthesis, schematic flow of solid phase peptide synthesis.
Chemistry of amino acids
The document provides information about amino acids and their classification. It discusses that amino acids are the monomer units that make up protein polymers. They can be classified based on their structure, side chains, nutritional requirements, and metabolic fate. The 20 standard amino acids are discussed in detail, including their physical and chemical properties. Key reactions of amino acids involving their amino, carboxyl, and side chain groups are also summarized.
Lipid200 structure and function
Lipids are a diverse group of compounds that are insoluble in water but soluble in organic solvents. They include fats, oils, waxes, sterols, and phospholipids. The document discusses the structure, function, and classification of various lipids. It describes simple lipids like triglycerides and waxes, as well as complex lipids including phospholipids. Phospholipids are important structural components of cell membranes and contain a phosphate group, alcohol, and fatty acids. Glycerophospholipids are the major class of phospholipids, with phosphatidylcholine, phosphatidylethanolamine, and others playing important roles in cells and tissues.
What's hot (20)
Amino acid -Classification of amino acid, Properties, peptides-Types and bio...
Amino acid -Classification of amino acid, Properties, peptides-Types and bio...
Complex Lipids (Phosholipids, Glycolipids and Lipoproteins) (Chemistry of Lip...
Complex Lipids (Phosholipids, Glycolipids and Lipoproteins) (Chemistry of Lip...
Amino acids and Protein chemistry by Dr. Anurag Yadav
Amino acids and Protein chemistry by Dr. Anurag Yadav
Similar to Polypeptides,peptides, types of peptides, structure of dipeptide, tripeptide and oligopeptide and different functions of peptide
Peptide by KK Sahu sir
Introduction
Definition
Structure of peptide bond
Classes
Dipeptides
Tripeptides
Polypeptides
Peptide synthesis
Liquid phase synthesis
Solid phase synthesis
General principle
Steps
Peptide overview
Application
Conclusion
References
peptides proteins ppt
Peptides and proteins are composed of chains of amino acids linked by peptide bonds. Peptides contain 2-50 amino acids while proteins have 50 or more. The primary structure of a peptide or protein refers to the specific sequence of amino acids. This sequence can be determined through amino acid composition analysis and methods like terminal residue analysis and partial hydrolysis, which selectively label and remove amino acids from the termini to reveal the sequence one by one. Determining the primary structure is important as changes in just one amino acid can impact structure and function.
Determination of primary structure of proteins
The document discusses the determination of the primary structure of proteins. It begins by explaining that proteins are composed of amino acid residues linked by peptide bonds to form a polypeptide chain. The primary structure refers to the specific sequence of amino acids in this chain. Mass spectrometry and tandem mass spectrometry techniques are used to analyze protein fragments obtained through enzymatic or chemical cleavage to determine the amino acid sequence and thereby elucidate the primary structure.
Peptides
Peptides are formed by the condensation of amino acids through peptide bonds. They have an N-terminus and C-terminus. Peptide bonds have partial double bond character due to resonance, restricting their rotation. The primary structure of proteins can be determined through acid hydrolysis and amino acid analysis. Techniques like ion-exchange chromatography and electrophoresis are used to separate amino acids. Edman degradation and carboxypeptidase digestion help identify terminal residues. Solid phase peptide synthesis improves on solution phase methods.
AP BIO Ch 5 ppt
Here are the names of the bonds:
1. Sugars in a polysaccharide - Glycosidic bonds
2. Amino acids in a protein - Peptide bonds
3. Nucleotides in a nucleic acid - Phosphodiester bonds
Protein structural analysis
This document discusses protein structure and analysis. It defines proteins as biomolecules composed of amino acid chains that differ from other molecules by containing nitrogen. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure refers to the amino acid sequence. Secondary structures include alpha helices and beta sheets formed by hydrogen bonds between amino acids. Tertiary structure describes the three-dimensional folding of the polypeptide. Quaternary structure is the arrangement of multiple protein subunits. Protein domains and interactions like disulfide bridges stabilize tertiary structures.
What are Peptides Difference between Peptides and Proteine
At Peptides 411 you get the entire scoop. What are peptides? The difference between Peptides and Proteins. Where to buy peptides and how to get the lowest prices.
Unit-2.pptx
The document discusses protein structure and function. It covers the following key points:
1) Amino acids are the building blocks of proteins. There are 20 common amino acids that make up proteins through peptide bond formation.
2) Protein structure is hierarchical, consisting of primary, secondary, tertiary, and sometimes quaternary levels. Secondary structure includes alpha helices and beta sheets formed by hydrogen bonding. Tertiary structure is determined by interactions between amino acid side chains.
3) Proteins are classified based on solubility, composition, and derivation. Simple proteins hydrolyze to amino acids, while conjugated proteins also contain non-protein components like lipids, sugars, or metals. Derived proteins result from
Cell Chemistry
Cells are the basic units of living organisms and contain organic molecules enclosed in a membrane. Macromolecules like carbohydrates, lipids, proteins and nucleic acids are made of smaller repeating units called monomers that polymerize. Proteins are polymers of amino acids linked by peptide bonds, while nucleic acids DNA and RNA are polymers of nucleotides consisting of a nitrogenous base, sugar and phosphate. They both play essential roles in storing and expressing genetic information.
Macromolecules Lecture
The document summarizes the key macromolecules that make up living things: carbohydrates, lipids, proteins, and nucleic acids. It describes how each is made of monomers that polymerize through condensation reactions, and how their structures determine their functions. Carbohydrates include sugars and starches used for energy storage. Lipids include fats and phospholipids that store energy and make up cell membranes. Proteins have complex 4-level structures (primary to quaternary) that allow for their diverse functions like transport and muscle movement. Nucleic acids DNA and RNA contain nucleotides and code or aid in protein synthesis to pass on traits.
Lec 2 level 3-nu(structure of protein)
Proteins have four levels of structural organization: primary, secondary, tertiary, and quaternary. The primary structure refers to the linear sequence of amino acids in the polypeptide chain. Secondary structure involves local folding patterns like alpha helices and beta sheets. Tertiary structure describes the overall 3D shape of a single polypeptide chain. Quaternary structure is the 3D structure formed by the assembly of multiple polypeptide subunits. The structures at each level are stabilized by interactions between the R groups of amino acids in the chain.
Ashok protein chemistry
This document discusses protein structure and synthesis. It begins by defining proteins and peptides, and the 20 amino acids that make up proteins. It then describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structure results from hydrogen bonding within the chain, forming structures like alpha helices. Tertiary structure describes the final 3D shape from chain folding. Quaternary structure involves the interaction of multiple peptide chains in an oligomeric protein. The document also outlines peptide bond formation and different peptide synthesis methods.
Jangid protein_chemistry_
This document discusses protein structure and synthesis. It begins by defining proteins and peptides, and the 20 amino acids that make up proteins. It then describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structure results from hydrogen bonding within the chain, forming structures like alpha helices. Tertiary structure describes the final 3D shape from chain folding. Quaternary structure involves the interaction of multiple peptide chains in an oligomeric protein. The document also outlines peptide bond formation and different peptide synthesis methods.
biology.pptx
Protein, RNA and DNA are made up of smaller building blocks. Protein is made from amino acids that are linked through peptide bonds. RNA and DNA are made from nucleotides that contain a phosphate group, a sugar (ribose in RNA and deoxyribose in DNA), and a nitrogenous base. There are four levels of protein structure - primary, secondary, tertiary and quaternary. RNA and DNA store and transmit genetic information through their structures and functions such as replication, transcription and translation.
non ribosomal peptide synthesis (molecular biology)
Non-ribosomal peptides are synthesized by large enzyme complexes called nonribosomal peptide synthetases. These synthetases are independent of mRNA and each can produce only one peptide. Nonribosomal peptides often contain non-proteinogenic amino acids and modifications like methyl groups. They have a diverse range of biological activities including being antibiotics, siderophores, toxins, and pigments. Nonribosomal peptide synthesis involves amino acid activation, attachment to carrier proteins, elongation via peptide bond formation, and termination through hydrolysis or cyclization.
primary structure of proteins by ifrah.pptx
1. The document discusses the primary structure of proteins, which is the linear sequence of amino acids that make up the polypeptide chain.
2. Determining the primary structure involves identifying the amino acid composition through acid hydrolysis, and sequencing the amino acids through methods like Edman degradation or by using enzymes like carboxypeptidase.
3. Understanding the primary structure is important because the sequence of amino acids determines a protein's function, and many genetic diseases are caused by changes to this sequence.
Biomolecule Examples
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Example
Amino acids and protein
Amino acids are organic compounds containing amino and carboxylic acid groups. There are about 300 amino acids in nature but only 20 are found in proteins. Amino acids are linked together via peptide bonds to form polypeptide chains and proteins. There are four levels of protein structure - primary, secondary, tertiary, and quaternary - that determine a protein's shape and function. Proteins can be classified as simple proteins which break down into amino acids, or conjugated proteins which break down into a protein and non-protein component like lipids or carbohydrates.
Lecture 5 bio
This document discusses the structure and function of macromolecules. It focuses on proteins, which are polymers of amino acids that fold into complex shapes to perform various functions in the body. The four levels of protein structure are described as primary, secondary, tertiary, and quaternary. Lipids are also covered, with details about their hydrophobic nature and roles as fats, phospholipids in cell membranes, and steroids like cholesterol.
16. Which of the following are generally true about Gram negative cel.pdf
16. Which of the following are generally true about Gram negative cell envelope? a.
Lipopolysaccharide is covalently attached to the N-acetylmuramic acid. b. There is periplasmic
space. c. Peptidoglycan is linked with B-1,3-glycosidic bonds. d. Interbridge strengthens the
peptidoglycan layer.
Solution
The cell envelope of Gram-negative bacteria has three principal layers: the outer membrane
(OM), the peptidoglycan cell wall, and the cytoplasmic or inner membrane (IM).
The OM is a lipid bilayer, not a phospholipid bilayer. It contains lipopolysaccharides,
lipoproteins, proteins and phospholipids. The outer leaflet of the OM is composed of glycolipids,
predominantly lipopolysaccharide (LPS).
Peptidoglycan cell wall:. The gram-negative bacteria has a thin (2-7 nm) peptidoglycan layer in
their cell wall. Peptidoglycan is a polymer made up of repeating units of the disaccharide N-
acetyl glucosamine (NAG) and -N-actyl muramic acid (NAM), cross-linked by -1,4 glycosidic
bond. NAM is NAG with a lactic acid linked through ether group. A tetrapeptide chain of four
alternating D- and L- aminoacids (L -alanine, D-alanine, D-glutamic acid and L-lysine/ meso
diamino-pimelic acid) is connected to the carboxyl group of the NAM. The two tetrapeptide
chains lying side by side may be linked together directly to each other or indirectly by a peptide
interbridge, of short chain aminoacids through transpeptidation. In addition to the peptidoglycan
layer the gram-negative cell wall also contains an additional outer membrane composed by
phospholipids and lipopolysaccharides.
The OM iscovalently joined to the underlying peptidoglycan by the abundant lipoprotein,
Lpp/murein lipoprotein, or Braun\'s lipoprotein. In addition, proteins such as OmpA bind with
peptidoglycan noncovalently.
The OM and IM define an aqueous cellular compartment/space called the periplasm with densely
packed proteins such as RNAse , alkaline phosphatase, periplasmic binding proteins (for sugar
and amino acid transport and chemotaxis).
The IM is a phospholipid bilayer, comprising mainly phosphatidyl ethanolamine and
phosphatidyl glycerol. The proteins that function in energy production, lipid biosynthesis, protein
secretion, and transport are located in the IM.
So based on the above inference, the true statements are:
b. There is periplasmic space
d. Interbridge strenghtens the peptidoglycan layer..
Similar to Polypeptides,peptides, types of peptides, structure of dipeptide, tripeptide and oligopeptide and different functions of peptide (20)
What are Peptides Difference between Peptides and Proteine
What are Peptides Difference between Peptides and Proteine
non ribosomal peptide synthesis (molecular biology)
non ribosomal peptide synthesis (molecular biology)
16. Which of the following are generally true about Gram negative cel.pdf
16. Which of the following are generally true about Gram negative cel.pdf
More from ShwetaMishra115
Classification & qualitative tests of amino acids
Classification & qualitative tests of amino acids
Classification based on nutrition, structure and polarity
Color reaction of amino acids, ninhydrin test, millions test, sakaguchi test, lead acetate test
Chemistry of proteins, primary structure, secondary structure,alpha-helical s...
chemistry of proteins, primary structure, secondary structure,alpha-helical structure , beta-pleated sheet,parallel pleated sheet, anti-parallel sheet, tertiary structure, Quaternary structure
Qualitative tests of proteins, color reaction of proteins,biuret's test, colo...
Qualitative tests of proteins
color reaction of proteins
biuret's test, color reaction of proteins, millon's test, ninhydrin test, qualitative tests of proteins, sakaguchi test, sodium nitroprusside test, xanthoproteic test
Deficiency diseases of proteins, kwashiorkor, marasmus
Kwashiorkor and marasmus are protein deficiency diseases that primarily affect children. Kwashiorkor occurs when children switch from breastfeeding to a low protein diet, causing symptoms like pigmentation, vomiting, and edema. Marasmus occurs due to a very low protein and calorie diet, leading to weight loss, diarrhea, and respiratory infections. Both diseases are diagnosed through physical exams and tests. Treatment focuses on increasing protein intake through foods like milk, eggs, and soy for kwashiorkor, and increasing overall protein, calories, and nutrients for marasmus.
Classification of proteins
Proteins can be classified in several ways:
1. Based on composition - such as albumins, globulins, glycoproteins, etc. Simple proteins contain only amino acids, conjugated proteins contain non-protein groups, and derived proteins are modified from natural proteins.
2. Based on structure - globular proteins have a spherical shape like enzymes and hormones, while fibrous proteins have a fiber-like structure like collagen.
3. Based on function - enzymic proteins show catalytic activity, structural proteins form tissues, transport proteins move molecules in the body, storage proteins store nutrients, and toxic proteins provide protection against pathogens.
Introduction to biochemistry
introduction to protein
objective of protein
importance of protein in medicine
scope of protein
biomolecules
Proteins part 2
This document discusses the role and function of proteins as well as their biological value. It outlines that proteins are primarily used in the body to build, maintain and repair tissues. They also produce enzymes, provide structure, act as hormones, store substances, and help with muscle contraction and blood coagulation. The biological value of a protein refers to the percentage of absorbed nitrogen that is retained in the body, and is a measure of protein quality. High biological value proteins include meat, eggs, milk, fish and cheese, while low biological value proteins include cereals, nuts, pulses and bread.
Proteins part 1
This document provides an introduction to proteins, including:
- Proteins are composed of amino acids joined by peptide bonds to form polypeptide chains. They are essential to the structure and function of tissues.
- Key components of proteins include carbon, hydrogen, oxygen, nitrogen and sometimes sulfur. Properties include solubility in water/acids/alkalies and hydrolysis into amino acids.
- Examples of protein-rich foods are listed like eggs, milk, meat, fish, nuts and beans. The document defines proteins and discusses their essential roles in the body.
Introduction to clinical pharmacy practice definition & scope
Clinical pharmacy involves pharmacists participating in patient care by providing drug information to healthcare professionals and patients. It aims to ensure patient well-being and safe, rational drug use. Clinical pharmacists take medication histories, monitor for drug interactions and adverse reactions, assist in drug selection and therapy, educate patients, and provide drug information to support optimal health outcomes. The scope of clinical pharmacy includes managing drug therapy for chronic conditions, controlling drug use, counseling patients, and collaborating with physicians and nurses through various educational and consultation activities.
Common daily terminology used in the practice of medicine (1) (1)
This document provides information on common medical terminology used in pharmacy practice. It begins by classifying terminology into four categories: dosage forms, pharmacological glossary, Latin terms, and miscellaneous. Under dosage forms, it lists and defines various solid, liquid, and semi-solid dosage forms. The pharmacological glossary section defines medical conditions, symptoms, and other terms. Common Latin abbreviations used in prescriptions are also explained. Finally, it briefly discusses generic drug names, brand names, over-the-counter drugs, and contraindications.
More from ShwetaMishra115 (10)
Chemistry of proteins, primary structure, secondary structure,alpha-helical s...
Chemistry of proteins, primary structure, secondary structure,alpha-helical s...
Qualitative tests of proteins, color reaction of proteins,biuret's test, colo...
Qualitative tests of proteins, color reaction of proteins,biuret's test, colo...
Deficiency diseases of proteins, kwashiorkor, marasmus
Deficiency diseases of proteins, kwashiorkor, marasmus
Introduction to clinical pharmacy practice definition & scope
Introduction to clinical pharmacy practice definition & scope
Common daily terminology used in the practice of medicine (1) (1)
Common daily terminology used in the practice of medicine (1) (1)
Recently uploaded
RPMS TEMPLATE FOR SCHOOL YEAR 2023-2024 FOR TEACHER 1 TO TEACHER 3
RPMS Template 2023-2024 by: Irene S. Rueco
The History of Stoke Newington Street Names
Presented at the Stoke Newington Literary Festival on 9th June 2024
www.StokeNewingtonHistory.com
Advanced Java[Extra Concepts, Not Difficult].docx
This is part 2 of my Java Learning Journey. This contains Hashing, ArrayList, LinkedList, Date and Time Classes, Calendar Class and more.
How to Setup Warehouse & Location in Odoo 17 Inventory
In this slide, we'll explore how to set up warehouses and locations in Odoo 17 Inventory. This will help us manage our stock effectively, track inventory levels, and streamline warehouse operations.
Community pharmacy- Social and preventive pharmacy UNIT 5
Covered community pharmacy topic of the subject Social and preventive pharmacy for Diploma and Bachelor of pharmacy
ISO/IEC 27001, ISO/IEC 42001, and GDPR: Best Practices for Implementation and...
Denis is a dynamic and results-driven Chief Information Officer (CIO) with a distinguished career spanning information systems analysis and technical project management. With a proven track record of spearheading the design and delivery of cutting-edge Information Management solutions, he has consistently elevated business operations, streamlined reporting functions, and maximized process efficiency.
Certified as an ISO/IEC 27001: Information Security Management Systems (ISMS) Lead Implementer, Data Protection Officer, and Cyber Risks Analyst, Denis brings a heightened focus on data security, privacy, and cyber resilience to every endeavor.
His expertise extends across a diverse spectrum of reporting, database, and web development applications, underpinned by an exceptional grasp of data storage and virtualization technologies. His proficiency in application testing, database administration, and data cleansing ensures seamless execution of complex projects.
What sets Denis apart is his comprehensive understanding of Business and Systems Analysis technologies, honed through involvement in all phases of the Software Development Lifecycle (SDLC). From meticulous requirements gathering to precise analysis, innovative design, rigorous development, thorough testing, and successful implementation, he has consistently delivered exceptional results.
Throughout his career, he has taken on multifaceted roles, from leading technical project management teams to owning solutions that drive operational excellence. His conscientious and proactive approach is unwavering, whether he is working independently or collaboratively within a team. His ability to connect with colleagues on a personal level underscores his commitment to fostering a harmonious and productive workplace environment.
Date: May 29, 2024
Tags: Information Security, ISO/IEC 27001, ISO/IEC 42001, Artificial Intelligence, GDPR
-------------------------------------------------------------------------------
Find out more about ISO training and certification services
Training: ISO/IEC 27001 Information Security Management System - EN | PECB
ISO/IEC 42001 Artificial Intelligence Management System - EN | PECB
General Data Protection Regulation (GDPR) - Training Courses - EN | PECB
Webinars: https://pecb.com/webinars
Article: https://pecb.com/article
-------------------------------------------------------------------------------
For more information about PECB:
Website: https://pecb.com/
LinkedIn: https://www.linkedin.com/company/pecb/
Facebook: https://www.facebook.com/PECBInternational/
Slideshare: http://www.slideshare.net/PECBCERTIFICATION
Azure Interview Questions and Answers PDF By ScholarHat
Azure Interview Questions and Answers PDF By ScholarHat
Natural birth techniques - Mrs.Akanksha Trivedi Rama University
Natural birth techniques - Mrs.Akanksha Trivedi Rama UniversityAkanksha trivedi rama nursing college kanpur.
Natural birth techniques are various type such as/ water birth , alexender method, hypnosis, bradley method, lamaze method etcExecutive Directors Chat Leveraging AI for Diversity, Equity, and Inclusion
Let’s explore the intersection of technology and equity in the final session of our DEI series. Discover how AI tools, like ChatGPT, can be used to support and enhance your nonprofit's DEI initiatives. Participants will gain insights into practical AI applications and get tips for leveraging technology to advance their DEI goals.
BÀI TẬP BỔ TRỢ TIẾNG ANH 8 CẢ NĂM - GLOBAL SUCCESS - NĂM HỌC 2023-2024 (CÓ FI...
BÀI TẬP BỔ TRỢ TIẾNG ANH 8 CẢ NĂM - GLOBAL SUCCESS - NĂM HỌC 2023-2024 (CÓ FI...Nguyen Thanh Tu Collection
https://app.box.com/s/y977uz6bpd3af4qsebv7r9b7s21935vdThe simplified electron and muon model, Oscillating Spacetime: The Foundation...
Discover the Simplified Electron and Muon Model: A New Wave-Based Approach to Understanding Particles delves into a groundbreaking theory that presents electrons and muons as rotating soliton waves within oscillating spacetime. Geared towards students, researchers, and science buffs, this book breaks down complex ideas into simple explanations. It covers topics such as electron waves, temporal dynamics, and the implications of this model on particle physics. With clear illustrations and easy-to-follow explanations, readers will gain a new outlook on the universe's fundamental nature.
Walmart Business+ and Spark Good for Nonprofits.pdf
"Learn about all the ways Walmart supports nonprofit organizations.
You will hear from Liz Willett, the Head of Nonprofits, and hear about what Walmart is doing to help nonprofits, including Walmart Business and Spark Good. Walmart Business+ is a new offer for nonprofits that offers discounts and also streamlines nonprofits order and expense tracking, saving time and money.
The webinar may also give some examples on how nonprofits can best leverage Walmart Business+.
The event will cover the following::
Walmart Business + (https://business.walmart.com/plus) is a new shopping experience for nonprofits, schools, and local business customers that connects an exclusive online shopping experience to stores. Benefits include free delivery and shipping, a 'Spend Analytics” feature, special discounts, deals and tax-exempt shopping.
Special TechSoup offer for a free 180 days membership, and up to $150 in discounts on eligible orders.
Spark Good (walmart.com/sparkgood) is a charitable platform that enables nonprofits to receive donations directly from customers and associates.
Answers about how you can do more with Walmart!"
LAND USE LAND COVER AND NDVI OF MIRZAPUR DISTRICT, UP
This Dissertation explores the particular circumstances of Mirzapur, a region located in the
core of India. Mirzapur, with its varied terrains and abundant biodiversity, offers an optimal
environment for investigating the changes in vegetation cover dynamics. Our study utilizes
advanced technologies such as GIS (Geographic Information Systems) and Remote sensing to
analyze the transformations that have taken place over the course of a decade.
The complex relationship between human activities and the environment has been the focus
of extensive research and worry. As the global community grapples with swift urbanization,
population expansion, and economic progress, the effects on natural ecosystems are becoming
more evident. A crucial element of this impact is the alteration of vegetation cover, which plays a
significant role in maintaining the ecological equilibrium of our planet.Land serves as the foundation for all human activities and provides the necessary materials for
these activities. As the most crucial natural resource, its utilization by humans results in different
'Land uses,' which are determined by both human activities and the physical characteristics of the
land.
The utilization of land is impacted by human needs and environmental factors. In countries
like India, rapid population growth and the emphasis on extensive resource exploitation can lead
to significant land degradation, adversely affecting the region's land cover.
Therefore, human intervention has significantly influenced land use patterns over many
centuries, evolving its structure over time and space. In the present era, these changes have
accelerated due to factors such as agriculture and urbanization. Information regarding land use and
cover is essential for various planning and management tasks related to the Earth's surface,
providing crucial environmental data for scientific, resource management, policy purposes, and
diverse human activities.
Accurate understanding of land use and cover is imperative for the development planning
of any area. Consequently, a wide range of professionals, including earth system scientists, land
and water managers, and urban planners, are interested in obtaining data on land use and cover
changes, conversion trends, and other related patterns. The spatial dimensions of land use and
cover support policymakers and scientists in making well-informed decisions, as alterations in
these patterns indicate shifts in economic and social conditions. Monitoring such changes with the
help of Advanced technologies like Remote Sensing and Geographic Information Systems is
crucial for coordinated efforts across different administrative levels. Advanced technologies like
Remote Sensing and Geographic Information Systems
9
Changes in vegetation cover refer to variations in the distribution, composition, and overall
structure of plant communities across different temporal and spatial scales. These changes can
occur natural.
clinical examination of hip joint (1).pdf
described clinical examination all orthopeadic conditions .
How to Make a Field Mandatory in Odoo 17
In Odoo, making a field required can be done through both Python code and XML views. When you set the required attribute to True in Python code, it makes the field required across all views where it's used. Conversely, when you set the required attribute in XML views, it makes the field required only in the context of that particular view.
Recently uploaded (20)
RPMS TEMPLATE FOR SCHOOL YEAR 2023-2024 FOR TEACHER 1 TO TEACHER 3
RPMS TEMPLATE FOR SCHOOL YEAR 2023-2024 FOR TEACHER 1 TO TEACHER 3
How to Setup Warehouse & Location in Odoo 17 Inventory
How to Setup Warehouse & Location in Odoo 17 Inventory
Pride Month Slides 2024 David Douglas School District
Pride Month Slides 2024 David Douglas School District
Community pharmacy- Social and preventive pharmacy UNIT 5
Community pharmacy- Social and preventive pharmacy UNIT 5
ISO/IEC 27001, ISO/IEC 42001, and GDPR: Best Practices for Implementation and...
ISO/IEC 27001, ISO/IEC 42001, and GDPR: Best Practices for Implementation and...
Azure Interview Questions and Answers PDF By ScholarHat
Azure Interview Questions and Answers PDF By ScholarHat
Natural birth techniques - Mrs.Akanksha Trivedi Rama University
Natural birth techniques - Mrs.Akanksha Trivedi Rama University
Executive Directors Chat Leveraging AI for Diversity, Equity, and Inclusion
Executive Directors Chat Leveraging AI for Diversity, Equity, and Inclusion
BÀI TẬP BỔ TRỢ TIẾNG ANH 8 CẢ NĂM - GLOBAL SUCCESS - NĂM HỌC 2023-2024 (CÓ FI...
BÀI TẬP BỔ TRỢ TIẾNG ANH 8 CẢ NĂM - GLOBAL SUCCESS - NĂM HỌC 2023-2024 (CÓ FI...
The simplified electron and muon model, Oscillating Spacetime: The Foundation...
The simplified electron and muon model, Oscillating Spacetime: The Foundation...
Walmart Business+ and Spark Good for Nonprofits.pdf
Walmart Business+ and Spark Good for Nonprofits.pdf
LAND USE LAND COVER AND NDVI OF MIRZAPUR DISTRICT, UP
LAND USE LAND COVER AND NDVI OF MIRZAPUR DISTRICT, UP
Polypeptides,peptides, types of peptides, structure of dipeptide, tripeptide and oligopeptide and different functions of peptide
- 1. BIOCHEMISTRY & CLINICAL PATHOLOGY TOPIC- POLYPEPTIDES PRESENTED BY- SHWETA MISHRA
- 2. POLYPEPTIDE ● Peptides are short polymers of amino acids(monomer) linked by peptide bonds between two molecules when the carboxyl group of one molecules reacts with the amino group of other molecule. ● Polypeptide are formed by long peptide chain containing large numbers of peptide bonds. ● Peptide bond is written as-CONH. ● One end of every polypeptide called the amino terminal or N- terminal, has free amino group. ● Other end, with its free carboxyl group, is called the carboxyl terminal or C-terminal.
- 4. DIPEPTIDE: A molecule containing two amino acids joint by a peptide bond called dipeptide. TRIPEPTIDE: A molecule containing three amino acids joint by a peptide bond called tripeptide. OLIGOPEPTIDE: A molecule containing few residue(less than 20) of amino acids joint by a peptide bond called oligopeptide.
- 5. Structure of Oligopeptide Structure of Dipeptide & Tripeptide
- 6. FUNCTIONS OF PEPTIDE BOND ● Proteins have a wide range of functions in the human body. ● Peptides are important in muscle building. For example, GHRP peptide is one of the finest Human Growth Hormone releasers. ● Peptides are also capable of raising prolactin hormone especially in females.(vasoactive intestinal peptide (VIP)). ● Copper based peptides are responsible for giving us flawless skin and protecting us from harsh sunny conditions. ● Some peptides like IPAMORELIN are also used to treat hunger issues. ● Peptides are also used to treat injuries. For example, HEXARELIN peptide has a pretty attractive healing potential.
- 7. THANK YOU