This document provides an overview of proteins and amino acids. It discusses the 20 standard amino acids that make up proteins, how they are joined by peptide bonds, and how amino acids are classified. It also outlines several important roles of proteins in biological processes, including enzymatic catalysis, transport, mechanical support, and growth regulation.
Classification and Structure of Standard Amino AcidsPalakAgrawal97
This document discusses the classification and structure of standard amino acids. It begins with an introduction to proteins and amino acids. It then covers the history of amino acid discoveries. The main body discusses the general structure of amino acids and various methods of classifying them, including by structure, polarity, nutritional requirements, and metabolic fate. It also briefly introduces selenocysteine as the 21st amino acid and the potential 22nd amino acid pyrrolysine. The document concludes that amino acids are essential for all life processes and metabolic functions.
1. The document discusses the chemistry of amino acids, which are the building blocks of proteins. It defines amino acids and their basic structure, and classifies them as standard and non-standard amino acids.
2. Amino acids are classified based on the nature of their side chains as hydrophobic, hydrophilic, positively charged, or negatively charged. Their side chains determine their properties and allow some amino acids to perform specific roles in proteins.
3. The document also discusses the essential, non-essential, and semi-essential amino acids based on nutritional requirements, and classifies amino acids as glucogenic, ketogenic, or both based on their metabolic fate.
This document discusses amino acids, which are the building blocks of proteins. It defines amino acids as molecules containing both carboxyl and amine groups. There are over 300 amino acids found in nature, but only 22 are used as the standard building blocks in proteins. These standard amino acids differ in the side chain (R group) attached to their alpha carbon. Amino acids join together via peptide bonds to form protein chains. Proteins are essential to all living organisms and are formed through the process of translation.
biosynthesis of amino acids, carbohydratesshallu kotwal
This document discusses the biosynthesis of amino acids. It begins with an introduction to amino acids, their general structure, and their physical and chemical properties. It then discusses peptides and peptide bonds. The main topics covered are:
1. Amino acids are synthesized through reductive amination of alpha-ketocids or the formation of glutamine amides. Glutamate and glutamine provide the critical entry points for incorporating ammonium ions.
2. Living organisms differ in their ability to synthesize amino acids. Plants and microorganisms can produce all 20, while mammals must obtain 8 essential amino acids from their diet.
3. There are two principal means of incorporating ammonium ions into amino acids -
The document discusses amino acids and proteins. It begins by listing the learning objectives, which include describing the 20 common amino acids, their structure and classification, as well as the structure and functions of peptides and proteins. It then defines amino acids as the building blocks of proteins, notes that 20 are commonly found in mammalian proteins, and describes their basic structure with an amino group, carboxyl group, hydrogen, and side chain. The document further classifies amino acids based on their chemical, nutritional, and metabolic properties and functions. It also explains how amino acids polymerize to form peptides and proteins, and the levels of structure in proteins from primary to quaternary.
This document discusses amino acids and peptides. It defines amino acids as organic acids that contain both an amino group and a carboxyl group attached to the same carbon atom. Proteins are polymers of amino acids linked together by peptide bonds. There are over 300 amino acids but only 20 are common in mammalian proteins. Amino acids are classified in different ways, and some are essential while others are non-essential. Peptides are formed when the carboxyl group of one amino acid reacts with the amino group of another, linking them together. The peptide bond gives proteins their structure and is important biologically.
Proteins are the major components of the body and are composed of amino acids. There are over 50,000 different proteins in the human body, each with a unique structure and function. Proteins serve many essential roles such as structure, movement, transport, regulation, and protection. They exhibit properties like solubility, ionization, hydration, and buffering capacity that allow them to perform their diverse functions. Proteins can be globular or fibrous in shape, and their molecular masses range from 5,500 to over 2 million Daltons depending on the number of amino acids.
1. The document discusses amino acid and protein metabolism. It covers topics like the amino acid pool, transamination, deamination, the metabolism of ammonia, and the urea cycle.
2. Transamination is the process where the amino group is transferred from one amino acid to a keto acid, catalyzed by transaminase enzymes. Deamination results in the liberation of ammonia for urea synthesis and the conversion of the amino acid carbon skeleton into a keto acid.
3. Glutamate plays a central role as it can accept amino groups via transamination and also undergo oxidative deamination to release ammonia via glutamate dehydrogenase. This links amino acid and urea metabolism to the TCA
Classification and Structure of Standard Amino AcidsPalakAgrawal97
This document discusses the classification and structure of standard amino acids. It begins with an introduction to proteins and amino acids. It then covers the history of amino acid discoveries. The main body discusses the general structure of amino acids and various methods of classifying them, including by structure, polarity, nutritional requirements, and metabolic fate. It also briefly introduces selenocysteine as the 21st amino acid and the potential 22nd amino acid pyrrolysine. The document concludes that amino acids are essential for all life processes and metabolic functions.
1. The document discusses the chemistry of amino acids, which are the building blocks of proteins. It defines amino acids and their basic structure, and classifies them as standard and non-standard amino acids.
2. Amino acids are classified based on the nature of their side chains as hydrophobic, hydrophilic, positively charged, or negatively charged. Their side chains determine their properties and allow some amino acids to perform specific roles in proteins.
3. The document also discusses the essential, non-essential, and semi-essential amino acids based on nutritional requirements, and classifies amino acids as glucogenic, ketogenic, or both based on their metabolic fate.
This document discusses amino acids, which are the building blocks of proteins. It defines amino acids as molecules containing both carboxyl and amine groups. There are over 300 amino acids found in nature, but only 22 are used as the standard building blocks in proteins. These standard amino acids differ in the side chain (R group) attached to their alpha carbon. Amino acids join together via peptide bonds to form protein chains. Proteins are essential to all living organisms and are formed through the process of translation.
biosynthesis of amino acids, carbohydratesshallu kotwal
This document discusses the biosynthesis of amino acids. It begins with an introduction to amino acids, their general structure, and their physical and chemical properties. It then discusses peptides and peptide bonds. The main topics covered are:
1. Amino acids are synthesized through reductive amination of alpha-ketocids or the formation of glutamine amides. Glutamate and glutamine provide the critical entry points for incorporating ammonium ions.
2. Living organisms differ in their ability to synthesize amino acids. Plants and microorganisms can produce all 20, while mammals must obtain 8 essential amino acids from their diet.
3. There are two principal means of incorporating ammonium ions into amino acids -
The document discusses amino acids and proteins. It begins by listing the learning objectives, which include describing the 20 common amino acids, their structure and classification, as well as the structure and functions of peptides and proteins. It then defines amino acids as the building blocks of proteins, notes that 20 are commonly found in mammalian proteins, and describes their basic structure with an amino group, carboxyl group, hydrogen, and side chain. The document further classifies amino acids based on their chemical, nutritional, and metabolic properties and functions. It also explains how amino acids polymerize to form peptides and proteins, and the levels of structure in proteins from primary to quaternary.
This document discusses amino acids and peptides. It defines amino acids as organic acids that contain both an amino group and a carboxyl group attached to the same carbon atom. Proteins are polymers of amino acids linked together by peptide bonds. There are over 300 amino acids but only 20 are common in mammalian proteins. Amino acids are classified in different ways, and some are essential while others are non-essential. Peptides are formed when the carboxyl group of one amino acid reacts with the amino group of another, linking them together. The peptide bond gives proteins their structure and is important biologically.
Proteins are the major components of the body and are composed of amino acids. There are over 50,000 different proteins in the human body, each with a unique structure and function. Proteins serve many essential roles such as structure, movement, transport, regulation, and protection. They exhibit properties like solubility, ionization, hydration, and buffering capacity that allow them to perform their diverse functions. Proteins can be globular or fibrous in shape, and their molecular masses range from 5,500 to over 2 million Daltons depending on the number of amino acids.
1. The document discusses amino acid and protein metabolism. It covers topics like the amino acid pool, transamination, deamination, the metabolism of ammonia, and the urea cycle.
2. Transamination is the process where the amino group is transferred from one amino acid to a keto acid, catalyzed by transaminase enzymes. Deamination results in the liberation of ammonia for urea synthesis and the conversion of the amino acid carbon skeleton into a keto acid.
3. Glutamate plays a central role as it can accept amino groups via transamination and also undergo oxidative deamination to release ammonia via glutamate dehydrogenase. This links amino acid and urea metabolism to the TCA
Amino acids are organic compounds that contain an amino group and a carboxyl group. There are 20 different amino acids that serve as the building blocks of proteins. Amino acids link together through peptide bonds to form polypeptide chains that fold into complex three-dimensional protein structures. Proteins serve essential functions and 10 of the 20 amino acids must be obtained through diet as humans cannot synthesize them. Common protein tests identify the presence of proteins using reactions that detect peptide bonds, amino acid side chains, or disulfide bridges.
Proteins are composed of amino acids linked together by peptide bonds. There are 20 standard amino acids, of which 9 are essential and must be obtained through diet. Amino acids combine to form polypeptides and proteins, which take on unique 3D structures that determine their specific functions. Protein digestion breaks down proteins into amino acids so they can be absorbed and used for various purposes throughout the body.
The document summarizes a biochemistry group project on proteins. The group, led by Mohammad Raes, discussed the definition, chemistry, structure, classification, properties, and functions of proteins. Key points included that proteins are polymers of amino acids and have four levels of structure - primary, secondary, tertiary, and quaternary. Proteins perform important roles such as enzymes, hormones, antibodies, and structure.
This document provides information about amino acids, peptides, and proteins. It discusses how proteins are the most abundant and functionally diverse molecules in living systems, performing essential roles like enzymatic functions and muscle movement. It describes the common components of amino acids, including carboxyl groups, amino groups, and variable side chains. Twenty amino acids are most commonly found in mammalian proteins. The document classifies these 20 amino acids and discusses their properties, including how nonpolar amino acids cluster inside proteins. It also covers cysteine and cystine, disulfide bonds, and properties of amino acids like solubility and acid-base characteristics. The polymerization of amino acids via peptide bonds to form polypeptides and proteins is also summarized.
Proteins are essential macromolecules that make up 20% of the human body. They are composed of amino acids and perform many critical functions including structure, regulation, catalysis, movement and more. Protein synthesis occurs in ribosomes within cells. Proteins are not stored but are broken down if excess amino acids are consumed. They have primary, secondary, tertiary and quaternary levels of structure determined by amino acid sequence and interactions. There are 20 standard amino acids that are linked by peptide bonds to form proteins.
This document discusses the ionization and pH of amino acids. It begins by providing background on amino acids, noting they contain both amine and carboxylic acid functional groups. It then discusses how amino acids can be classified, including by their side chains. Neutral, acidic, and basic side chains are described. PKa values and isoelectric points are also discussed. The document provides examples of glycine ionization and discusses zwitterion formation in amino acids. Tables of amino acid properties including pKa values and molecular weights are also included.
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.
This document discusses proteins, including their structure, types, and functions. It notes that proteins are composed of amino acids, of which there are 20 common types. Proteins can have fibrous or globular structures depending on how the polypeptide chains are arranged. The structures of proteins include primary, secondary, tertiary, and sometimes quaternary structures. Examples of protein functions include digestion, transport, structure, signaling, defense, and storage. The document also discusses amino acid classification, protein denaturation, and the mechanism of enzyme catalysis.
The document discusses the structure and properties of amino acids. It notes that amino acids are the building blocks of proteins and contain both an amino group and a carboxyl group. There are 20 standard amino acids that are used in protein synthesis. Amino acids share a common core structure but differ in their variable side chains. They can be classified based on the polarity of their side chains and whether they are essential or non-essential to humans. The document also discusses the nomenclature and abbreviations of amino acids, as well as some specialized amino acids like selenocysteine.
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.
This document discusses the chemistry of amino acids and proteins. It defines proteins and amino acids, describing how amino acids are the building blocks of proteins. It classifies amino acids based on their structure, metabolic fate, side chains, and nutritional status. Essential amino acids cannot be synthesized in the body, while non-essential amino acids can. The document also categorizes proteins according to their function, shape and size, physical properties, and nutritional properties. Common protein types include enzymes, transport proteins, storage proteins, and structural proteins.
Proteins are composed of amino acids and play important structural and functional roles in the body. There are 20 standard amino acids that are used to build proteins through peptide bonds between amino and carboxyl groups. Proteins have primary, secondary, tertiary, and sometimes quaternary structures that determine their shape and function. Their structures are stabilized through hydrogen bonds, disulfide bridges, and other weak interactions. Denaturation disrupts these structures and causes proteins to lose their native 3D shapes and biological functions.
Proteins are the most abundant organic molecules in living systems and are made up of amino acids. They perform many important structural and functional roles. There are three main levels of protein structure - primary, secondary, and tertiary. The primary structure is the linear sequence of amino acids in the polypeptide chain. The secondary structure involves twisting of the chain into shapes like alpha helices and beta pleated sheets. Tertiary structure refers to the 3D conformation that a protein folds into. Some proteins have quaternary structure which involves the spatial arrangement of multiple polypeptide subunits.
This document discusses the chemistry of proteins. It begins by classifying proteins and their functions in organisms. It then discusses the structure and properties of amino acids, including their classification based on structure, polarity, nutrition requirements, and metabolic fate. It introduces peptides and peptide bonds. Key points are that proteins are composed of amino acids joined by peptide bonds, there are 20 standard amino acids, and proteins serve important structural and dynamic roles in organisms.
Proteins are composed of chains of amino acids and serve important structural and functional roles in biology. They can be classified based on their composition, structure, and biological function. Common analytical techniques used to study proteins include chromatography, electrophoresis, and mass spectrometry which separate proteins based on properties like size and charge. The diversity of amino acid side chains allows proteins to adopt complex 3D structures and perform a wide variety of critical roles in the body.
Proteins are composed of amino acids and play many essential roles in the body. They have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence, secondary involves hydrogen bonding into shapes like alpha helices and beta sheets, tertiary is the 3D folding of these structures, and quaternary involves the assembly of multiple protein subunits. Proteins serve as enzymes, hormones, antibodies, and structures. They undergo synthesis from amino acids and breakdown through catabolism. Disorders can occur if amino acid metabolism is disrupted.
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 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 have physical properties like solubility and melting points. Amino acids play important roles in many biological functions and reactions due to their amino, carboxyl, and side chain groups. They are essential for protein synthesis, cellular functions, and as precursors for other biomolecules.
This document provides an overview of a biochemistry course taught by Dr. Asmaa Saleh Ali. The course covers topics like amino acids and protein structure, lipids, carbohydrates, enzymes, vitamins, and metabolism over 11 weeks. Students will be assessed through two exams, class participation, and a final cumulative exam which together will make up 100% of their grade. The first lecture will introduce biochemistry and the basic biomolecules found in living organisms including an in-depth discussion of amino acids and protein structure.
This document discusses amino acids and their properties. It begins by explaining that amino acids are organic compounds that contain amine and carboxyl groups and have different R groups. Proteins are composed of chains of amino acids linked by peptide bonds. There are 20 standard amino acids that are the building blocks of proteins. The document then classifies amino acids based on their R groups and discusses their structures, chemical properties, and roles in the body.
This document discusses the mechanism and regulation of hydrochloric acid secretion in the stomach. It contains the following key points:
1) Hydrochloric acid is secreted by parietal cells in the stomach through an energy-requiring process that transports protons against a concentration gradient. This involves the K+-ATPase pump and generation of hydrogen ions from carbonic acid.
2) Gastrin and histamine are the main stimulators of acid secretion. Gastrin secretion is inhibited by acidic pH in a feedback loop.
3) Tests of gastric function include analysis of resting gastric contents, pentagastrin testing to measure maximal acid output, and insulin-induced hypoglycemia testing.
The document discusses peptic ulcer disease, specifically focusing on the role of Helicobacter pylori infection as the main cause of gastric and duodenal ulcers. It details how H. pylori infection increases the risk of gastric cancer and peptic ulcers. The document then discusses various diagnostic tests for H. pylori infection and peptic ulcer disease, including biopsy, urea breath tests, and stool antigen tests. It also discusses the recommended treatment of peptic ulcer disease when patients are infected with H. pylori.
Amino acids are organic compounds that contain an amino group and a carboxyl group. There are 20 different amino acids that serve as the building blocks of proteins. Amino acids link together through peptide bonds to form polypeptide chains that fold into complex three-dimensional protein structures. Proteins serve essential functions and 10 of the 20 amino acids must be obtained through diet as humans cannot synthesize them. Common protein tests identify the presence of proteins using reactions that detect peptide bonds, amino acid side chains, or disulfide bridges.
Proteins are composed of amino acids linked together by peptide bonds. There are 20 standard amino acids, of which 9 are essential and must be obtained through diet. Amino acids combine to form polypeptides and proteins, which take on unique 3D structures that determine their specific functions. Protein digestion breaks down proteins into amino acids so they can be absorbed and used for various purposes throughout the body.
The document summarizes a biochemistry group project on proteins. The group, led by Mohammad Raes, discussed the definition, chemistry, structure, classification, properties, and functions of proteins. Key points included that proteins are polymers of amino acids and have four levels of structure - primary, secondary, tertiary, and quaternary. Proteins perform important roles such as enzymes, hormones, antibodies, and structure.
This document provides information about amino acids, peptides, and proteins. It discusses how proteins are the most abundant and functionally diverse molecules in living systems, performing essential roles like enzymatic functions and muscle movement. It describes the common components of amino acids, including carboxyl groups, amino groups, and variable side chains. Twenty amino acids are most commonly found in mammalian proteins. The document classifies these 20 amino acids and discusses their properties, including how nonpolar amino acids cluster inside proteins. It also covers cysteine and cystine, disulfide bonds, and properties of amino acids like solubility and acid-base characteristics. The polymerization of amino acids via peptide bonds to form polypeptides and proteins is also summarized.
Proteins are essential macromolecules that make up 20% of the human body. They are composed of amino acids and perform many critical functions including structure, regulation, catalysis, movement and more. Protein synthesis occurs in ribosomes within cells. Proteins are not stored but are broken down if excess amino acids are consumed. They have primary, secondary, tertiary and quaternary levels of structure determined by amino acid sequence and interactions. There are 20 standard amino acids that are linked by peptide bonds to form proteins.
This document discusses the ionization and pH of amino acids. It begins by providing background on amino acids, noting they contain both amine and carboxylic acid functional groups. It then discusses how amino acids can be classified, including by their side chains. Neutral, acidic, and basic side chains are described. PKa values and isoelectric points are also discussed. The document provides examples of glycine ionization and discusses zwitterion formation in amino acids. Tables of amino acid properties including pKa values and molecular weights are also included.
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.
This document discusses proteins, including their structure, types, and functions. It notes that proteins are composed of amino acids, of which there are 20 common types. Proteins can have fibrous or globular structures depending on how the polypeptide chains are arranged. The structures of proteins include primary, secondary, tertiary, and sometimes quaternary structures. Examples of protein functions include digestion, transport, structure, signaling, defense, and storage. The document also discusses amino acid classification, protein denaturation, and the mechanism of enzyme catalysis.
The document discusses the structure and properties of amino acids. It notes that amino acids are the building blocks of proteins and contain both an amino group and a carboxyl group. There are 20 standard amino acids that are used in protein synthesis. Amino acids share a common core structure but differ in their variable side chains. They can be classified based on the polarity of their side chains and whether they are essential or non-essential to humans. The document also discusses the nomenclature and abbreviations of amino acids, as well as some specialized amino acids like selenocysteine.
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.
This document discusses the chemistry of amino acids and proteins. It defines proteins and amino acids, describing how amino acids are the building blocks of proteins. It classifies amino acids based on their structure, metabolic fate, side chains, and nutritional status. Essential amino acids cannot be synthesized in the body, while non-essential amino acids can. The document also categorizes proteins according to their function, shape and size, physical properties, and nutritional properties. Common protein types include enzymes, transport proteins, storage proteins, and structural proteins.
Proteins are composed of amino acids and play important structural and functional roles in the body. There are 20 standard amino acids that are used to build proteins through peptide bonds between amino and carboxyl groups. Proteins have primary, secondary, tertiary, and sometimes quaternary structures that determine their shape and function. Their structures are stabilized through hydrogen bonds, disulfide bridges, and other weak interactions. Denaturation disrupts these structures and causes proteins to lose their native 3D shapes and biological functions.
Proteins are the most abundant organic molecules in living systems and are made up of amino acids. They perform many important structural and functional roles. There are three main levels of protein structure - primary, secondary, and tertiary. The primary structure is the linear sequence of amino acids in the polypeptide chain. The secondary structure involves twisting of the chain into shapes like alpha helices and beta pleated sheets. Tertiary structure refers to the 3D conformation that a protein folds into. Some proteins have quaternary structure which involves the spatial arrangement of multiple polypeptide subunits.
This document discusses the chemistry of proteins. It begins by classifying proteins and their functions in organisms. It then discusses the structure and properties of amino acids, including their classification based on structure, polarity, nutrition requirements, and metabolic fate. It introduces peptides and peptide bonds. Key points are that proteins are composed of amino acids joined by peptide bonds, there are 20 standard amino acids, and proteins serve important structural and dynamic roles in organisms.
Proteins are composed of chains of amino acids and serve important structural and functional roles in biology. They can be classified based on their composition, structure, and biological function. Common analytical techniques used to study proteins include chromatography, electrophoresis, and mass spectrometry which separate proteins based on properties like size and charge. The diversity of amino acid side chains allows proteins to adopt complex 3D structures and perform a wide variety of critical roles in the body.
Proteins are composed of amino acids and play many essential roles in the body. They have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence, secondary involves hydrogen bonding into shapes like alpha helices and beta sheets, tertiary is the 3D folding of these structures, and quaternary involves the assembly of multiple protein subunits. Proteins serve as enzymes, hormones, antibodies, and structures. They undergo synthesis from amino acids and breakdown through catabolism. Disorders can occur if amino acid metabolism is disrupted.
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 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 have physical properties like solubility and melting points. Amino acids play important roles in many biological functions and reactions due to their amino, carboxyl, and side chain groups. They are essential for protein synthesis, cellular functions, and as precursors for other biomolecules.
This document provides an overview of a biochemistry course taught by Dr. Asmaa Saleh Ali. The course covers topics like amino acids and protein structure, lipids, carbohydrates, enzymes, vitamins, and metabolism over 11 weeks. Students will be assessed through two exams, class participation, and a final cumulative exam which together will make up 100% of their grade. The first lecture will introduce biochemistry and the basic biomolecules found in living organisms including an in-depth discussion of amino acids and protein structure.
This document discusses amino acids and their properties. It begins by explaining that amino acids are organic compounds that contain amine and carboxyl groups and have different R groups. Proteins are composed of chains of amino acids linked by peptide bonds. There are 20 standard amino acids that are the building blocks of proteins. The document then classifies amino acids based on their R groups and discusses their structures, chemical properties, and roles in the body.
This document discusses the mechanism and regulation of hydrochloric acid secretion in the stomach. It contains the following key points:
1) Hydrochloric acid is secreted by parietal cells in the stomach through an energy-requiring process that transports protons against a concentration gradient. This involves the K+-ATPase pump and generation of hydrogen ions from carbonic acid.
2) Gastrin and histamine are the main stimulators of acid secretion. Gastrin secretion is inhibited by acidic pH in a feedback loop.
3) Tests of gastric function include analysis of resting gastric contents, pentagastrin testing to measure maximal acid output, and insulin-induced hypoglycemia testing.
The document discusses peptic ulcer disease, specifically focusing on the role of Helicobacter pylori infection as the main cause of gastric and duodenal ulcers. It details how H. pylori infection increases the risk of gastric cancer and peptic ulcers. The document then discusses various diagnostic tests for H. pylori infection and peptic ulcer disease, including biopsy, urea breath tests, and stool antigen tests. It also discusses the recommended treatment of peptic ulcer disease when patients are infected with H. pylori.
This document discusses peptic ulcer disease and its main cause, Helicobacter pylori bacteria. It notes that H. pylori infection is present in about half of the world's population and increases the risk of gastric cancer and peptic ulcers. At least 95% of duodenal ulcer patients are infected with H. pylori. The document discusses various tests used to diagnose H. pylori infection, including urea breath tests and biopsy tests. Eradication of H. pylori through treatment is recommended for patients with peptic ulcers who test positive for the infection.
Spectrophotometry and colorimetry are analytical techniques that use light to determine properties of substances. Spectrophotometry measures how much light is absorbed by a solution and can be used to determine concentration. It works by passing light through a sample and measuring the absorption at specific wavelengths. Many factors can affect the measurements, including concentration, path length, and calibration. Spectrophotometry has wide applications in fields like chemistry, medicine, food science and more.
This document discusses the principles and applications of nephelometry and turbidimetry. Both methods measure the scattering of light by particles in solution, but differ in how the scattered light is measured. Nephelometry measures scattered light at an angle, usually 90 degrees, to the incident light beam. Turbidimetry measures light transmitted through the solution in the direction of the incident beam. Factors that affect scattering include particle concentration, size, shape, wavelength of light, and refractive indices of particles and solvent. Applications include determining concentrations of substances like proteins, sulfate, and ammonia in biochemical and environmental analysis.
The document discusses hemoglobin synthesis, which consists of two parts: globin synthesis and heme synthesis. Globin is synthesized through transcription and translation of genes on chromosomes 16 and 11. Heme is synthesized through the Shemin cycle, where glycine and succinyl-CoA are condensed to form delta-aminolevulinic acid, which undergoes further modifications to ultimately form protoporphyrin IX. Protoporphyrin then binds iron to form heme. Heme synthesis is regulated by feedback inhibition of delta-aminolevulinic acid synthase, and both heme and globin are required for the formation of functional hemoglobin.
This document discusses the structure and function of haemoglobin and the transport of gases in the blood. It provides a history of discoveries about haemoglobin dating back to the 17th century. Key points covered include the tetrameric structure of haemoglobin, with each subunit binding one heme group and iron atom. Haemoglobin is able to efficiently transport oxygen and carbon dioxide via changes in its quaternary structure and binding of effectors like hydrogen ions, carbon dioxide and 2,3-BPG. The sigmoidal oxygen dissociation curve illustrates haemoglobin's ability to load and unload oxygen in the lungs and tissues respectively. Factors like pH, temperature and organic phosphates influence the curve.
This document discusses pilot studies and pretesting of surveys. It defines a pilot study as a small-scale trial of the research process to assess feasibility, while pretesting specifically refers to testing survey questions to ensure they are clear and understood by respondents. The key objectives of pilot studies and pretesting are to validate research tools and methods, identify any issues, and improve the quality and rigor of the full research project. Sample sizes of 10-30% of the planned study are typically used for pilot testing.
This document discusses carbohydrates, including their classification, roles, and functions. Carbohydrates can be classified as monosaccharides, disaccharides, oligosaccharides, or polysaccharides based on the number of sugar units present. Examples of monosaccharides are glucose and galactose. Important polysaccharides include glycogen, starch, and cellulose. Carbohydrates serve important structural and metabolic roles, such as providing energy, storing energy as glycogen, detoxifying the body, and being components of genetic material and cellular structures.
Local Advanced Lung Cancer: Artificial Intelligence, Synergetics, Complex Sys...Oleg Kshivets
Overall life span (LS) was 1671.7±1721.6 days and cumulative 5YS reached 62.4%, 10 years – 50.4%, 20 years – 44.6%. 94 LCP lived more than 5 years without cancer (LS=2958.6±1723.6 days), 22 – more than 10 years (LS=5571±1841.8 days). 67 LCP died because of LC (LS=471.9±344 days). AT significantly improved 5YS (68% vs. 53.7%) (P=0.028 by log-rank test). Cox modeling displayed that 5YS of LCP significantly depended on: N0-N12, T3-4, blood cell circuit, cell ratio factors (ratio between cancer cells-CC and blood cells subpopulations), LC cell dynamics, recalcification time, heparin tolerance, prothrombin index, protein, AT, procedure type (P=0.000-0.031). Neural networks, genetic algorithm selection and bootstrap simulation revealed relationships between 5YS and N0-12 (rank=1), thrombocytes/CC (rank=2), segmented neutrophils/CC (3), eosinophils/CC (4), erythrocytes/CC (5), healthy cells/CC (6), lymphocytes/CC (7), stick neutrophils/CC (8), leucocytes/CC (9), monocytes/CC (10). Correct prediction of 5YS was 100% by neural networks computing (error=0.000; area under ROC curve=1.0).
Basavarajeeyam is an important text for ayurvedic physician belonging to andhra pradehs. It is a popular compendium in various parts of our country as well as in andhra pradesh. The content of the text was presented in sanskrit and telugu language (Bilingual). One of the most famous book in ayurvedic pharmaceutics and therapeutics. This book contains 25 chapters called as prakaranas. Many rasaoushadis were explained, pioneer of dhatu druti, nadi pareeksha, mutra pareeksha etc. Belongs to the period of 15-16 century. New diseases like upadamsha, phiranga rogas are explained.
Muktapishti is a traditional Ayurvedic preparation made from Shoditha Mukta (Purified Pearl), is believed to help regulate thyroid function and reduce symptoms of hyperthyroidism due to its cooling and balancing properties. Clinical evidence on its efficacy remains limited, necessitating further research to validate its therapeutic benefits.
Promoting Wellbeing - Applied Social Psychology - Psychology SuperNotesPsychoTech Services
A proprietary approach developed by bringing together the best of learning theories from Psychology, design principles from the world of visualization, and pedagogical methods from over a decade of training experience, that enables you to: Learn better, faster!
Rasamanikya is a excellent preparation in the field of Rasashastra, it is used in various Kushtha Roga, Shwasa, Vicharchika, Bhagandara, Vatarakta, and Phiranga Roga. In this article Preparation& Comparative analytical profile for both Formulationon i.e Rasamanikya prepared by Kushmanda swarasa & Churnodhaka Shodita Haratala. The study aims to provide insights into the comparative efficacy and analytical aspects of these formulations for enhanced therapeutic outcomes.
Adhd Medication Shortage Uk - trinexpharmacy.comreignlana06
The UK is currently facing a Adhd Medication Shortage Uk, which has left many patients and their families grappling with uncertainty and frustration. ADHD, or Attention Deficit Hyperactivity Disorder, is a chronic condition that requires consistent medication to manage effectively. This shortage has highlighted the critical role these medications play in the daily lives of those affected by ADHD. Contact : +1 (747) 209 – 3649 E-mail : sales@trinexpharmacy.com
NVBDCP.pptx Nation vector borne disease control programSapna Thakur
NVBDCP was launched in 2003-2004 . Vector-Borne Disease: Disease that results from an infection transmitted to humans and other animals by blood-feeding arthropods, such as mosquitoes, ticks, and fleas. Examples of vector-borne diseases include Dengue fever, West Nile Virus, Lyme disease, and malaria.
Does Over-Masturbation Contribute to Chronic Prostatitis.pptxwalterHu5
In some case, your chronic prostatitis may be related to over-masturbation. Generally, natural medicine Diuretic and Anti-inflammatory Pill can help mee get a cure.
2. LESSON OBJECTIVES
At the end of this lesson you will have an
understanding of,
the general structure of α- amino acids
the 20 amino acids which make up proteins
the chemical nature of amino acids,
different ways of classifying amino acids and proteins,
formation of peptide bonds and
the role of proteins in biological process.
3. INTRODUCTION
Amino acids are the basic structural units of proteins.
Proteins in all species from bacteria to humans are made
from the same set of twenty amino acids.
Amino acids take part in many types of reactions, but the
most important of these is the formation of a peptide
bond.
This involves the joining of the α- carboxyl group of one
amino acid to the α-amino group of another amino acid,
with the loss of a water molecule.
5. CHEMICAL NATURE OF AMINO ACIDS
An amino acid consists of amino group (NH2), a
carboxyl group (-COOH), a hydrogen atom (H)
and a distinctive R group bonded to a carbon
atom, called the α- carbon.
The R group is specific to each amino acid.
Amino acids in solution at neutral pH
are predominantly dipolar ions also called
a Zwitterions.
6. CHEMICAL NATURE OF AMINO ACIDS
In the dipolar form, the amino group is
protonated (-NH3
+) while the carboxyl
group is dissociated (-COO-).
The ionization state of an amino acid varies
with pH.
At physiological pH, carboxyl groups exist
almost entirely as -COO- and amino groups
predominantly as -NH3+
8. THE 20 AMINO ACIDS FOUND IN PROTEINS
Proteins found in living organisms contain only
twenty (20) different kinds of amino acids.
The same 20 standard amino acids make up the
proteins in all living cell either in virus, bacteria,
yeast, plant or human cell.
These 20 amino acids combine in different
sequences and numbers to form various kinds of
proteins.
The table below shows the 20 standard amino
acids.
11. CLASSIFICATION OF AMINO ACIDS
Amino acids are classified based on;
1. Nutritional requirement (Essential, non-
essential, semi-essential)
2. The fate of each amino acid in mammals
(glucogenic, ketogenic)
3. Charge (neutral, acidic, basic)
12. CLASSIFICATION BASED ON NUTRITIONAL
REQUIREMENT
1. Essential amino acids (EAA)
Are amino acids that cannot be
synthesized by the human body, and
therefore have to be supplied by the diet.
EAA are also known as indispensable
amino acids.
13. CLASSIFICATION BASED ON NUTRITIONAL
REQUIREMENT
2. Non-Essential amino acids (EAA)
Are amino acids that can be synthesized by
the body are called non-essential amino
acids (dispensable amino acids).
14. CLASSIFICATION BASED ON NUTRITIONAL
REQUIREMENT
Out of the 20 common amino acids, 10 are
essential while the other 10 are non-essential.
Daily adult intake of amino acids is
approximately 0.8g/Kg.
This will be higher for a child or pregnant woman.
Dietary proteins cannot be absorbed directly from
the intestine. They must be hydrolyzed by a
group of enzymes (proteases and peptidases) to
amino acids.
15. CLASSIFICATION BASED ON NUTRITIONAL
REQUIREMENT
3. Semi-essential Amino Acids
These are amino acids that can be synthesized
within the organism but their synthesis is not in
sufficient amounts, however they should also be
provided in the diet.
Two amino acids are grouped under semi-essential
amino acids and they are Arginine and Histidine.
16. CLASSIFICATION BASED ON THE FATE OF
EACH AMINO ACID IN MAMMALS
Amino acids can be classified as glucogenic (i.e.
potentially can be converted to glucose),
ketogenic (i.e. potentially be converted to
ketone bodies).
17. CLASSIFICATION BASED ON THE FATE OF
EACH AMINO ACID IN MAMMALS
1.GLUCOGENIC AMINO ACIDS
Glucogenic amino acids are amino acids in
which their carbon skeleton gets degraded to
pyruvate, α ketoglutarate, succinyl CoA,
fumarate and oxaloacetate and then converted
to glucose and glycogen.
These include alanine, cysteine, glycine,
arginine, glutamine, isoleucine, and tyrosine.
18. CLASSIFICATION BASED ON THE FATE OF
EACH AMINO ACID IN MAMMALS
2. KETOGENIC AMINO ACIDS
These are amino acids in which their carbon
skeleton is degraded to acetoacetyl CoA, or
acetyl CoA and then get converted to acetone
and β-hydroxy butyrate which are referred to
ketone bodies.
These include phenylalanine, tyrosine,
tryptophan, isoleucine, leucine, and lysine.
19. CLASSIFICATION BASED ON THE FATE OF
EACH AMINO ACID IN MAMMALS
2. KETOGENIC AMINO ACIDS
These amino acids have the ability to form
ketone bodies which is particularly evident in
untreated diabetes mellitus in which large
amounts of ketone bodies are produced by
the liver.
Degradation of leucine which is an exclusively
ketogenic amino acid makes a substantial
contribution to the formation of ketone
bodies especially during starvation.
20. CLASSIFICATION DEPENDING ON THE
CHARGE
1. NEUTRAL AMINO ACIDS
These are amino acids that do not contain any
charge on the R group.
They are further classified into
Aliphatic amino acids which contains a chain
of carbon atoms e.g. Glycine, Alanine, Seine,
Threonine, Valine, Leucine, Isoleucine,
Asparagine, Glutamine
21. CLASSIFICATION DEPENDING ON THE
CHARGE
1. NEUTRAL AMINO ACIDS
Aromatic amino acid which have an aromatic
shape or contains benzene ring e.g.
Phenylalanine, Tyrosine, Tryptophan.
Heterocyclic amino acids which have
heterocyclic ring i.e. any of the ring structures
which contain different atoms.
Sulphur containing amino acids which are amino
acids which contain Sulphur atom e.g. Cysteine
and Methionine.
22. CLASSIFICATION DEPENDING ON THE
CHARGE
2. Acidic amino acids: These are amino acids
that contain a negative charge or an acidic
group e.g. Aspartate, Glutamate
3. Basic amino acids: These contain a positive
charge or a basic group e.g. Arginine, Lysine and
Histidine.
23. FORMATION OF PEPTIDE BONDS
The most important reaction of amino acids is
the formation of a peptide bond.
This involves the joining of the α-carboxyl group
of one amino acid to the α-amino group of
another amino acid, with resultant loss of a
water molecule.
Many amino acids (usually > 100) are joined by
peptide bonds to form a polypeptide chain.
24. CLASSIFICATION OF PROTEINS
Proteins are macromolecules with a
backbone formed by polymerization of
amino acids. They are nitrogenous
compounds of high molecular weight
which play a vital or prime role in living
organisms.
Proteins may be classified on the basis of
their composition, solubility, shape and
their biological functions
28. CLASSIFICATION OF PROTEINS BASED ON BIOLOGICAL
FUNCTIONS
Act as enzymes e.g. kinases, transaminases etc.
Act as storage proteins e.g. myoglobin, ferritin
Act as regulatory proteins e.g. peptide hormones,
DNA binding proteins
Act as structural proteins e.g. collagen,
proteoglycan
Act as protective proteins e.g. blood clotting
factors, immunoglobins (antibodies),
Act as transport protein e.g. hemoglobin, plasma
lipoproteins
Act as contractile or motile proteins e.g. actin,
tubulin
29. ROLES OF PROTEINS IN BIOLOGICAL
PROCESSES
Proteins play crucial roles in virtually all biological
processes.
Some of these roles include:
1. Enzymatic catalysis:
Nearly all chemical reactions in biological
systems are catalyzed by enzymes.
Most enzymes are proteins. Thus, proteins play
the unique role of determining the pattern of
chemical transformations in biological systems.
30. ROLES OF PROTEINS IN BIOLOGICAL
PROCESSES
2. Transport and storage
Many small molecules and ions are transported by
specific proteins e.g. Hb (hemoglobin)
transports oxygen in erythrocytes while
myoglobin transports oxygen in muscle.
Transferrin carries iron in the plasma of blood
to the liver where it is stored as a complex
with ferritin, another protein.
31. ROLES OF PROTEINS IN BIOLOGICAL
PROCESSES
3. Co-ordinated motion
Proteins are the major components of muscle.
Muscle contraction is accomplished by the sliding
motion of two kinds of protein filaments.
4. Mechanical support
The high tensile strength of skin and bone is due
to the presence of collage, a fibrous protein.
32. ROLES OF PROTEINS IN BIOLOGICAL
PROCESSES
5. Immune protection
Antibodies are highly specific proteins that
recognize and combine with foreign substances
such as viruses, bacteria and cells from other
organisms.
6. Generation and transmission of nerve
impulses:
The response of nerve cells to specific stimuli
is mediated by receptor proteins e.g.
rhodopsin is the photoreceptor protein in retinal
rod cells.
33. ROLES OF PROTEINS IN BIOLOGICAL
PROCESSES
7. Control of Growth and Differentiation:
Controlled sequential expression of genetic
information is essential for the orderly growth
and differentiation of cells.
Repressor proteins are important control
elements that silence specific segments of the
DNA of a cell.
Nerve growth factor, a protein complex serves to
guide the formation of neutral networks in higher
organisms.
34. CONCLUSION
Proteins are nitrogenous organic compounds
of high molecular weight which play a primary
role in living organisms.
They are polymers of amino acids and are
essential nutrients for tissue growth, repairs
and replacement.
35. STUDY QUESTIONS
1. Describe the chemical nature of amino
acids.
2. Explain the formation of peptide bond.
3. State the biological role of protein in the
living system.