protein.pptx-Biochemistry
•Download as PPTX, PDF•
1 like•1,516 views
Proteins are made up of building blocks called amino acids. There are about 20 different amino acids that link together in different combinations. Your body uses them to make new proteins, such as muscle and bone, and other compounds such as enzymes and hormones. It can also use them as an energy source.
Report
Share
Report
Share
Recommended
Carbohydrate metabolism
These are major source of energy for living organisms.
Supplying a huge array of metabolic intermediates for biosynthetic reactions.
The structural elements in cell coat or connective tissues.
Catabolism of heme
The document summarizes the catabolism of heme. Heme is degraded in reticuloendothelial cells of the liver, spleen, and bone marrow. It is broken down into biliverdin by heme oxygenase and then into bilirubin by biliverdin reductase. Bilirubin binds to albumin and is taken up by hepatocytes in the liver. In the liver, bilirubin is conjugated with glucuronic acid and excreted into bile. It is further broken down in the intestines into urobilinogen and stercobilinogen and excreted in urine and feces. Normal plasma bilirubin is 0.2-0.8
Metabolism of lipid
Subject : Nutrition, Unit- VI
This topic provides brief knowledge about lipid metabolism and it is prepared according to INC syllabus for first year BSc Nursing Students.
Fatty Acid metabolism
1. Beta oxidation of fatty acids occurs in the mitochondria and involves repeated cycles of condensation, hydration, dehydrogenation and thiolysis to ultimately produce acetyl-CoA.
2. Fatty acid synthesis occurs in the cytoplasm through a fatty acid synthase complex and utilizes acetyl-CoA and malonyl-CoA units to produce palmitate through cycles of condensation, reduction, dehydration and reduction.
3. Key differences between the pathways include site of action (mitochondria vs cytoplasm), use of CoA derivatives vs covalent linkage to ACP, and utilization of NAD+/FAD vs NADPH as electron carriers.
Lipoprotein
Lipoproteins are biochemical assemblies that transport hydrophobic lipid molecules in water and blood. They consist of a phospholipid and cholesterol outer shell with apolipoproteins embedded that stabilize the complex and determine its function. The main types of lipoproteins are chylomicrons, VLDL, IDL, LDL, and HDL, which differ in size, density, and lipid and protein composition. They enable the transport and metabolism of triglycerides, cholesterol, and other lipids throughout the body.
Proteins biochemistry
Proteins are composed of amino acids that link together via peptide bonds. There are 20 naturally occurring amino acids that vary in properties like polarity, charge, and ability to form secondary structures. The sequence and interactions of amino acids give proteins their unique 3D structures and functions. Denaturation disrupts non-covalent bonds within proteins, altering their shapes and eliminating biological activity.
DIGESTION & ABSORPTION OF LIPIDS
Lipids undergo a multi-step digestion and absorption process in the gastrointestinal tract. Dietary lipids are emulsified and broken down into smaller components like fatty acids and monoacylglycerols by lingual and gastric lipases in the stomach and pancreatic lipase in the small intestine. Bile salts produced by the liver play a key role in emulsification. The products of digestion are incorporated into micelles and absorbed by intestinal cells. Inside cells, fatty acids are reassembled into triglycerides and packaged into chylomicrons that enter the lymphatic system and bloodstream for transport to tissues. Defects in digestion, emulsification, or absorption can impair this process.
Digestion & absorption of proteins
This document summarizes the digestion and absorption of proteins in the human body. It discusses that proteins are obtained endogenously from digestive enzymes and cells, as well as exogenously from dietary intake. The stomach contains hydrochloric acid and pepsin to denature and break down proteins. The pancreas secretes trypsinogen, chymotrypsinogen, and other zymogens which are activated and further digest proteins into peptides and amino acids in the small intestine. Aminopeptidases and dipeptidases on intestinal cells complete the digestion. Amino acids are then absorbed via active transport systems involving sodium and ATP. Deficiencies or defects in these digestive processes can impair protein digestion.
Recommended
Carbohydrate metabolism
These are major source of energy for living organisms.
Supplying a huge array of metabolic intermediates for biosynthetic reactions.
The structural elements in cell coat or connective tissues.
Catabolism of heme
The document summarizes the catabolism of heme. Heme is degraded in reticuloendothelial cells of the liver, spleen, and bone marrow. It is broken down into biliverdin by heme oxygenase and then into bilirubin by biliverdin reductase. Bilirubin binds to albumin and is taken up by hepatocytes in the liver. In the liver, bilirubin is conjugated with glucuronic acid and excreted into bile. It is further broken down in the intestines into urobilinogen and stercobilinogen and excreted in urine and feces. Normal plasma bilirubin is 0.2-0.8
Metabolism of lipid
Subject : Nutrition, Unit- VI
This topic provides brief knowledge about lipid metabolism and it is prepared according to INC syllabus for first year BSc Nursing Students.
Fatty Acid metabolism
1. Beta oxidation of fatty acids occurs in the mitochondria and involves repeated cycles of condensation, hydration, dehydrogenation and thiolysis to ultimately produce acetyl-CoA.
2. Fatty acid synthesis occurs in the cytoplasm through a fatty acid synthase complex and utilizes acetyl-CoA and malonyl-CoA units to produce palmitate through cycles of condensation, reduction, dehydration and reduction.
3. Key differences between the pathways include site of action (mitochondria vs cytoplasm), use of CoA derivatives vs covalent linkage to ACP, and utilization of NAD+/FAD vs NADPH as electron carriers.
Lipoprotein
Lipoproteins are biochemical assemblies that transport hydrophobic lipid molecules in water and blood. They consist of a phospholipid and cholesterol outer shell with apolipoproteins embedded that stabilize the complex and determine its function. The main types of lipoproteins are chylomicrons, VLDL, IDL, LDL, and HDL, which differ in size, density, and lipid and protein composition. They enable the transport and metabolism of triglycerides, cholesterol, and other lipids throughout the body.
Proteins biochemistry
Proteins are composed of amino acids that link together via peptide bonds. There are 20 naturally occurring amino acids that vary in properties like polarity, charge, and ability to form secondary structures. The sequence and interactions of amino acids give proteins their unique 3D structures and functions. Denaturation disrupts non-covalent bonds within proteins, altering their shapes and eliminating biological activity.
DIGESTION & ABSORPTION OF LIPIDS
Lipids undergo a multi-step digestion and absorption process in the gastrointestinal tract. Dietary lipids are emulsified and broken down into smaller components like fatty acids and monoacylglycerols by lingual and gastric lipases in the stomach and pancreatic lipase in the small intestine. Bile salts produced by the liver play a key role in emulsification. The products of digestion are incorporated into micelles and absorbed by intestinal cells. Inside cells, fatty acids are reassembled into triglycerides and packaged into chylomicrons that enter the lymphatic system and bloodstream for transport to tissues. Defects in digestion, emulsification, or absorption can impair this process.
Digestion & absorption of proteins
This document summarizes the digestion and absorption of proteins in the human body. It discusses that proteins are obtained endogenously from digestive enzymes and cells, as well as exogenously from dietary intake. The stomach contains hydrochloric acid and pepsin to denature and break down proteins. The pancreas secretes trypsinogen, chymotrypsinogen, and other zymogens which are activated and further digest proteins into peptides and amino acids in the small intestine. Aminopeptidases and dipeptidases on intestinal cells complete the digestion. Amino acids are then absorbed via active transport systems involving sodium and ATP. Deficiencies or defects in these digestive processes can impair protein digestion.
Amino acid metabolism
The document discusses amino acid metabolism. It begins by defining amino acids as derivatives of carboxylic acids with an amino group substitution. Amino acids are essential for building proteins and participate in many metabolic reactions. They are classified by the properties of their side chains. Protein digestion involves proteases in the stomach, pancreas, and small intestine that hydrolyze proteins into amino acids. Amino acids are absorbed into the blood and transported to tissues. Within cells, amino groups are transferred between amino acids and ketoacids in transamination reactions or removed as ammonia by deamination. The liver converts ammonia into less toxic urea via the urea cycle to prevent intoxication. Defects in the urea cycle can
Nucleotide
This document discusses nucleotide chemistry. Nucleotides are organic compounds composed of a phosphate group, nitrogenous base, and a sugar molecule. They serve as the building blocks of nucleic acids DNA and RNA. Nucleotides also function as sources of chemical energy through molecules like ATP and GTP, and participate in cellular signaling through molecules like cAMP and cGMP. The document goes on to describe the specific sugars, bases, nucleosides, and nucleotides that make up DNA and RNA. It provides details on nucleotide nomenclature and classification and discusses important adenosine-containing nucleotides and their roles, such as ATP serving as an important energy source in many cellular processes.
Proteins (2)
Proteins are macromolecules made of amino acid polymers known as polypeptide chains. The sequence of amino acids in a protein is determined by the gene coding for that protein. Proteins perform essential functions in living cells such as catalyzing biochemical reactions as enzymes, regulating processes as hormones, transporting molecules, providing structure, and more. After synthesis, proteins are often modified with additional functional groups which can confer new abilities like recognizing other molecules or integrating into membranes.
Amino acids
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.
Digestion and absorption of lipids
The major dietary lipids are triacylglycerols, cholesterol, phospholipids, and free fatty acids. Lipids are insoluble in water and require digestion by lipases and emulsification by bile salts to be broken down into absorbable components. In the small intestine, pancreatic lipase breaks triacylglycerols into fatty acids and monoacylglycerols within mixed micelles. Bile salts also aid in emulsifying lipids into smaller particles. Digestion products are absorbed via micelle diffusion and resynthesized into triglycerides and phospholipids within intestinal cells before transport to the liver via the lymphatic system or blood.
Amino acid & Protein
This document discusses proteins and amino acids. It defines proteins as large biomolecules composed of chains of amino acids that are essential to life processes. The 20 standard amino acids are the building blocks of proteins. They contain an amino group, a carboxyl group, a hydrogen atom, and a variable side chain that determines each amino acid's properties. Proteins have primary, secondary, tertiary, and quaternary structures that give them their final 3D shapes and functions in the body.
Lipoproteins- structure, classification, metabolism and clinical significance
Lipoproteins transport lipids between cells and tissues. They consist of a nonpolar lipid core surrounded by a surface layer of phospholipids and proteins. Lipoproteins are classified based on density into chylomicrons, VLDL, IDL, LDL, and HDL. Chylomicrons transport dietary lipids from the intestine. The liver secretes VLDL, which circulates and is converted to IDL and LDL through lipolysis. HDL transports cholesterol from tissues to the liver. Apolipoproteins associated with each lipoprotein determine its function and metabolism.
Biological roles of proteins
Proteins play very significant role in cell functioning. they are known as workhorse of cell. they are made up of amino acids.
Biochemistry of Carbohydrates
This document provides information about carbohydrates. It discusses that carbohydrates are the most abundant organic molecules in nature and an important source of energy for cells. Carbohydrates can also act as structural components and be involved in cell membranes, surface antigens, and extracellular substances. The document further describes different types of carbohydrates including monosaccharides, disaccharides, and polysaccharides. It provides examples and characteristics of important carbohydrates such as glucose, fructose, sucrose, lactose, and glycogen. Reaction and derivatives of monosaccharides are also summarized.
CHOLESTEROL BIOSYNTHESIS
Cholesterol is synthesized from acetyl-CoA in a multi-step process located in the endoplasmic reticulum and cytoplasm. HMG-CoA reductase catalyzes the rate-limiting step and is regulated by transcription, covalent modification, and competitive inhibitors like statins. Cholesterol is transported by LDL and HDL and is used for cell membrane structure, steroid hormone synthesis, or storage.
Proteins
This document discusses proteins, including their structure, function, digestion, and importance. It notes that proteins are made up of amino acids and are essential for building muscle mass. During digestion, proteins are broken down into amino acids in the stomach and small intestine through chemical and mechanical processes aided by enzymes. The amino acids are then absorbed and transported to cells to build new proteins. Maintaining a variety of protein sources in the diet is important for health.
Beta-oxidation of fatty acids
This document provides information on beta-oxidation of fatty acids. It discusses the three stages of beta-oxidation: activation of fatty acids in the cytosol, transport into mitochondria via carnitine shuttle, and beta-oxidation in the mitochondrial matrix. The four reactions of each beta-oxidation cycle are also described: oxidation, hydration, oxidation, and cleavage. Deficiencies in beta-oxidation can cause conditions like sudden infant death syndrome.
Absorption of proteins ppt
Absorption of proteins ppt
composition of protein ppt
digestion of protein ppt
Absorption of protein ppt
absorption of amino acid ppt
function of protein ppt
amino acid ppt
role enzyme ppt
Lipids Notes
the slide contain detail note on:
1.Lipids
2.types of Lipids.
3.Function of Lipids
4.Chemical Composition of Lipids
etc etc
Classification and properties of protein
This document discusses the classification and properties of proteins. It describes four levels of protein structure: primary, secondary, tertiary, and quaternary. Proteins can also be classified by their biological function, which includes enzymes, transport proteins, storage proteins, contractile/motile proteins, structural proteins, defense proteins, regulatory proteins, and other functional proteins. Classification by shape and solubility includes fibrous, globular, and membrane proteins. Classification by composition distinguishes between simple and conjugated proteins. Nutritionally, proteins are either complete or incomplete. The document concludes by discussing properties like denaturation and its causes like heat, alcohol, acids, bases, and heavy metal salts.
Classification of Protein by different mode.
• Description: In this video the viewers will come to know about different mode of classification of proteins. Proteins are classified based on their Solubility and composition, Function, Shape & size.
Portion explained:
Classification based on solubility and composition
Simple proteins
1. Albumins
2. Globulins
3. Prolamins
4. Glutelins
5. Histones
6. Protamines
7. Albuminoids
ii. Conjugated or compound proteins
1. Nucleoproteins
2. Mucoproteins
3. Chromoproteins
4. Lipoproteins
5. Metalloproteins
6. Phosphoproteins
B. Classification of proteins based on function
1. Catalytic proteins – Enzymes
2. Regulatory proteins – Hormones
3. Protective proteins – Antibodies
4. Storage proteins
5. Transport proteins
6. Toxic proteins
7. Structural proteins
8. Contractile proteins
9. Secretary proteins
10. Exotic proteins
C. Classification based on size and shape
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.
PROTEIN STRUCTURE PRESENTATION
The document discusses the structure of proteins at various levels of organization:
- Proteins are composed of amino acids linked together by peptide bonds to form polypeptide chains. The sequence and interactions of these chains determine the protein's structure.
- There are four levels of protein structure - primary, secondary, tertiary, and quaternary. Secondary structure includes alpha helices and beta sheets formed by hydrogen bonding between amino acids in the chain. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure involves the interaction of multiple polypeptide chains.
- Protein structure enables proteins to perform their diverse functions through processes like enzyme catalysis, oxygen transport, and providing structure
Carbohydrates
Carbohydrates are biomolecules composed of carbon, hydrogen, and oxygen. They are classified as monosaccharides, oligosaccharides, or polysaccharides depending on the number of monomer units present. Monosaccharides include simple sugars like glucose and fructose. Disaccharides are formed from two monosaccharides joined by a glycosidic bond, examples being sucrose and lactose. Polysaccharides are polymers of monosaccharides and include starch, glycogen, and cellulose. Carbohydrates serve important functions as energy sources, structural components of cells and organisms, and precursors for other biomolecules.
proteins and its classification
This document discusses the classification and structure of proteins. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. The secondary structure involves local folding patterns stabilized by hydrogen bonds. The tertiary structure is the overall three-dimensional shape of a protein determined by interactions between amino acid side chains. Quaternary structure refers to the arrangement of multiple protein subunits. The document also categorizes proteins based on their biological functions and physical properties.
ankita parihar.pptx
This document discusses the structural hierarchy of proteins from primary to quaternary structure. It explains that proteins are made up of amino acids linked together in polypeptide chains. The primary structure is the sequence of amino acids in the chain. Secondary structures like alpha helices and beta sheets form due to hydrogen bonding. Tertiary structure is the 3D folding of secondary structures into the lowest energy state. Quaternary structure involves multiple polypeptide chains combining to form oligomeric proteins. The document also classifies proteins based on shape and constitution and discusses the functions of different types of proteins like enzymes, hormones, and structural proteins.
Protein metabolism.pptx
Proteins are the most abundant organic molecules of the living system.
They occur in every part of the cell and constitute about 50% of the cellular dry weight.
Proteins form the fundamental basis of structure and function of life.
Amino acids are the monomers that make up proteins
More Related Content
What's hot
Amino acid metabolism
The document discusses amino acid metabolism. It begins by defining amino acids as derivatives of carboxylic acids with an amino group substitution. Amino acids are essential for building proteins and participate in many metabolic reactions. They are classified by the properties of their side chains. Protein digestion involves proteases in the stomach, pancreas, and small intestine that hydrolyze proteins into amino acids. Amino acids are absorbed into the blood and transported to tissues. Within cells, amino groups are transferred between amino acids and ketoacids in transamination reactions or removed as ammonia by deamination. The liver converts ammonia into less toxic urea via the urea cycle to prevent intoxication. Defects in the urea cycle can
Nucleotide
This document discusses nucleotide chemistry. Nucleotides are organic compounds composed of a phosphate group, nitrogenous base, and a sugar molecule. They serve as the building blocks of nucleic acids DNA and RNA. Nucleotides also function as sources of chemical energy through molecules like ATP and GTP, and participate in cellular signaling through molecules like cAMP and cGMP. The document goes on to describe the specific sugars, bases, nucleosides, and nucleotides that make up DNA and RNA. It provides details on nucleotide nomenclature and classification and discusses important adenosine-containing nucleotides and their roles, such as ATP serving as an important energy source in many cellular processes.
Proteins (2)
Proteins are macromolecules made of amino acid polymers known as polypeptide chains. The sequence of amino acids in a protein is determined by the gene coding for that protein. Proteins perform essential functions in living cells such as catalyzing biochemical reactions as enzymes, regulating processes as hormones, transporting molecules, providing structure, and more. After synthesis, proteins are often modified with additional functional groups which can confer new abilities like recognizing other molecules or integrating into membranes.
Amino acids
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.
Digestion and absorption of lipids
The major dietary lipids are triacylglycerols, cholesterol, phospholipids, and free fatty acids. Lipids are insoluble in water and require digestion by lipases and emulsification by bile salts to be broken down into absorbable components. In the small intestine, pancreatic lipase breaks triacylglycerols into fatty acids and monoacylglycerols within mixed micelles. Bile salts also aid in emulsifying lipids into smaller particles. Digestion products are absorbed via micelle diffusion and resynthesized into triglycerides and phospholipids within intestinal cells before transport to the liver via the lymphatic system or blood.
Amino acid & Protein
This document discusses proteins and amino acids. It defines proteins as large biomolecules composed of chains of amino acids that are essential to life processes. The 20 standard amino acids are the building blocks of proteins. They contain an amino group, a carboxyl group, a hydrogen atom, and a variable side chain that determines each amino acid's properties. Proteins have primary, secondary, tertiary, and quaternary structures that give them their final 3D shapes and functions in the body.
Lipoproteins- structure, classification, metabolism and clinical significance
Lipoproteins transport lipids between cells and tissues. They consist of a nonpolar lipid core surrounded by a surface layer of phospholipids and proteins. Lipoproteins are classified based on density into chylomicrons, VLDL, IDL, LDL, and HDL. Chylomicrons transport dietary lipids from the intestine. The liver secretes VLDL, which circulates and is converted to IDL and LDL through lipolysis. HDL transports cholesterol from tissues to the liver. Apolipoproteins associated with each lipoprotein determine its function and metabolism.
Biological roles of proteins
Proteins play very significant role in cell functioning. they are known as workhorse of cell. they are made up of amino acids.
Biochemistry of Carbohydrates
This document provides information about carbohydrates. It discusses that carbohydrates are the most abundant organic molecules in nature and an important source of energy for cells. Carbohydrates can also act as structural components and be involved in cell membranes, surface antigens, and extracellular substances. The document further describes different types of carbohydrates including monosaccharides, disaccharides, and polysaccharides. It provides examples and characteristics of important carbohydrates such as glucose, fructose, sucrose, lactose, and glycogen. Reaction and derivatives of monosaccharides are also summarized.
CHOLESTEROL BIOSYNTHESIS
Cholesterol is synthesized from acetyl-CoA in a multi-step process located in the endoplasmic reticulum and cytoplasm. HMG-CoA reductase catalyzes the rate-limiting step and is regulated by transcription, covalent modification, and competitive inhibitors like statins. Cholesterol is transported by LDL and HDL and is used for cell membrane structure, steroid hormone synthesis, or storage.
Proteins
This document discusses proteins, including their structure, function, digestion, and importance. It notes that proteins are made up of amino acids and are essential for building muscle mass. During digestion, proteins are broken down into amino acids in the stomach and small intestine through chemical and mechanical processes aided by enzymes. The amino acids are then absorbed and transported to cells to build new proteins. Maintaining a variety of protein sources in the diet is important for health.
Beta-oxidation of fatty acids
This document provides information on beta-oxidation of fatty acids. It discusses the three stages of beta-oxidation: activation of fatty acids in the cytosol, transport into mitochondria via carnitine shuttle, and beta-oxidation in the mitochondrial matrix. The four reactions of each beta-oxidation cycle are also described: oxidation, hydration, oxidation, and cleavage. Deficiencies in beta-oxidation can cause conditions like sudden infant death syndrome.
Absorption of proteins ppt
Absorption of proteins ppt
composition of protein ppt
digestion of protein ppt
Absorption of protein ppt
absorption of amino acid ppt
function of protein ppt
amino acid ppt
role enzyme ppt
Lipids Notes
the slide contain detail note on:
1.Lipids
2.types of Lipids.
3.Function of Lipids
4.Chemical Composition of Lipids
etc etc
Classification and properties of protein
This document discusses the classification and properties of proteins. It describes four levels of protein structure: primary, secondary, tertiary, and quaternary. Proteins can also be classified by their biological function, which includes enzymes, transport proteins, storage proteins, contractile/motile proteins, structural proteins, defense proteins, regulatory proteins, and other functional proteins. Classification by shape and solubility includes fibrous, globular, and membrane proteins. Classification by composition distinguishes between simple and conjugated proteins. Nutritionally, proteins are either complete or incomplete. The document concludes by discussing properties like denaturation and its causes like heat, alcohol, acids, bases, and heavy metal salts.
Classification of Protein by different mode.
• Description: In this video the viewers will come to know about different mode of classification of proteins. Proteins are classified based on their Solubility and composition, Function, Shape & size.
Portion explained:
Classification based on solubility and composition
Simple proteins
1. Albumins
2. Globulins
3. Prolamins
4. Glutelins
5. Histones
6. Protamines
7. Albuminoids
ii. Conjugated or compound proteins
1. Nucleoproteins
2. Mucoproteins
3. Chromoproteins
4. Lipoproteins
5. Metalloproteins
6. Phosphoproteins
B. Classification of proteins based on function
1. Catalytic proteins – Enzymes
2. Regulatory proteins – Hormones
3. Protective proteins – Antibodies
4. Storage proteins
5. Transport proteins
6. Toxic proteins
7. Structural proteins
8. Contractile proteins
9. Secretary proteins
10. Exotic proteins
C. Classification based on size and shape
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.
PROTEIN STRUCTURE PRESENTATION
The document discusses the structure of proteins at various levels of organization:
- Proteins are composed of amino acids linked together by peptide bonds to form polypeptide chains. The sequence and interactions of these chains determine the protein's structure.
- There are four levels of protein structure - primary, secondary, tertiary, and quaternary. Secondary structure includes alpha helices and beta sheets formed by hydrogen bonding between amino acids in the chain. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure involves the interaction of multiple polypeptide chains.
- Protein structure enables proteins to perform their diverse functions through processes like enzyme catalysis, oxygen transport, and providing structure
Carbohydrates
Carbohydrates are biomolecules composed of carbon, hydrogen, and oxygen. They are classified as monosaccharides, oligosaccharides, or polysaccharides depending on the number of monomer units present. Monosaccharides include simple sugars like glucose and fructose. Disaccharides are formed from two monosaccharides joined by a glycosidic bond, examples being sucrose and lactose. Polysaccharides are polymers of monosaccharides and include starch, glycogen, and cellulose. Carbohydrates serve important functions as energy sources, structural components of cells and organisms, and precursors for other biomolecules.
proteins and its classification
This document discusses the classification and structure of proteins. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. The secondary structure involves local folding patterns stabilized by hydrogen bonds. The tertiary structure is the overall three-dimensional shape of a protein determined by interactions between amino acid side chains. Quaternary structure refers to the arrangement of multiple protein subunits. The document also categorizes proteins based on their biological functions and physical properties.
What's hot (20)
Lipoproteins- structure, classification, metabolism and clinical significance
Lipoproteins- structure, classification, metabolism and clinical significance
Similar to protein.pptx-Biochemistry
ankita parihar.pptx
This document discusses the structural hierarchy of proteins from primary to quaternary structure. It explains that proteins are made up of amino acids linked together in polypeptide chains. The primary structure is the sequence of amino acids in the chain. Secondary structures like alpha helices and beta sheets form due to hydrogen bonding. Tertiary structure is the 3D folding of secondary structures into the lowest energy state. Quaternary structure involves multiple polypeptide chains combining to form oligomeric proteins. The document also classifies proteins based on shape and constitution and discusses the functions of different types of proteins like enzymes, hormones, and structural proteins.
Protein metabolism.pptx
Proteins are the most abundant organic molecules of the living system.
They occur in every part of the cell and constitute about 50% of the cellular dry weight.
Proteins form the fundamental basis of structure and function of life.
Amino acids are the monomers that make up proteins
Proteins PPT final (1).pptx
Proteins are polymers of amino acids that perform essential functions in living organisms. They can be classified as simple, conjugated, or derived proteins based on their structure and components. Simple proteins like albumins and globulins are made of amino acids alone, while conjugated proteins also contain non-protein elements like nucleic acids or carbohydrates. Proteins have primary, secondary, tertiary, and quaternary levels of structure that determine their shape and function. They are found in all tissues and play critical roles including structure, movement, digestion, energy storage, and heredity.
Protein & Biochemical Role part 2
Proteins play many important biochemical roles in the body. They act as enzymes, hormones, antibodies, and structural components. Proteins can be classified based on their shape (fibrous or globular) or chemical composition (simple or conjugated). Simple proteins only contain amino acids, while conjugated proteins also contain non-amino acid groups like nucleic acids, lipids, carbohydrates, or metals. Proteins are further classified as complete or incomplete based on whether they contain all essential amino acids.
PROTEINS GROUP 2.pptx
This presentation discusses proteins and their functions. It defines proteins as nitrogenous compounds made of amino acids. Proteins perform many crucial functions in the body including growth, enzyme production, transport, defense, and maintenance of acid-base balance. The presentation covers protein structure, classification, sources, digestion and absorption. It emphasizes the importance of consuming complete proteins from both plant and animal sources to meet nutritional needs. Recommended daily intakes vary by age, gender and physiological state. Maintaining positive nitrogen balance is also discussed.
Protein classification function important
Protein is essential for building and repairing tissues, producing enzymes and hormones, and maintaining overall health. Good sources include meat, poultry, fish, eggs, dairy, legumes, nuts, and seeds. How can I assist you further with protein
Proteins can be classified based on various criteria, including their structure, function, and source. Structurally, proteins are categorized into four primary levels:
1. Primary structure: The sequence of amino acids in a protein chain.
2. Secondary structure: Local folding patterns such as alpha helices and beta sheets.
3. Tertiary structure: The overall 3D shape of the protein molecule.
4. Quaternary structure: The arrangement of multiple protein subunits, if applicable.
Functionally, proteins can be classified based on their roles in the body, such as enzymes, structural proteins, hormones, antibodies, transport proteins, and more.
Finally, proteins can also be classified based on their source, such as animal proteins (found in meat, dairy, eggs) and plant proteins (found in legumes, nuts, seeds). Let me know if you need more details on any specific classification!
Proteins play crucial roles in the body, serving as building blocks for tissues, enzymes for biochemical reactions, hormones for signaling, antibodies for immune defense, and transporters for molecules across cell membranes. Without adequate protein intake, various physiological functions would be impaired, leading to health issues. Thus, ensuring sufficient protein intake is essential for overall health and well-being.
Protein is an essential macronutrient in our diet, crucial for building and repairing tissues, supporting immune function, and regulating various processes in the body. In terms of nutrition, it's important to consume an adequate amount of protein daily, with recommendations varying based on factors like age, sex, weight, activity level, and overall health status.
For most adults, the recommended dietary allowance (RDA) for protein is around 0.8 grams per kilogram of body weight per day. However, individual protein needs may vary, and some individuals, such as athletes or those recovering from injury, may require higher protein intake.
It's also essential to consume a variety of protein sources to ensure you get all the essential amino acids your body needs. Good sources of protein include lean meats, poultry, fish, eggs, dairy products, legumes, nuts, seeds, and tofu.
Incorporating protein-rich foods into meals and snacks throughout the day can help maintain muscle mass, support satiety, and contribute to overall nutritional balance. If you have specific dietary goals or health concerns, consulting with a registered dietitian or nutritionist can help tailor your protein intake to meet your individual needs.
Dietary sources of protein include a wide range of foods, both from animal and plant sources. Here are some common examples:
1. **Animal Sources**:
- Meat: Beef, pork, lamb, veal, etc.
- Poultry: Chicken, tur
Lec.3protein chem.classification new microsoft powerpoint presentation
Proteins are complex biomolecules composed of amino acid chains that perform essential functions in the human body. They can be classified based on their composition, structure, and function. Some key types of proteins include structural proteins like collagen and keratin; transport proteins like hemoglobin; catalytic proteins which include enzymes; and regulatory proteins such as hormones. There are approximately 50,000 to 200,000 different proteins present in the human body, performing vital roles such as oxygen transport, muscle movement, immune defense, and metabolic processes.
Lec.3 protein chem.classification
Proteins are complex biomolecules composed of amino acid chains that perform essential functions in the human body. They can be classified based on their composition, structure, and function. Some key types of proteins include structural proteins like collagen and keratin; transport proteins like hemoglobin; catalytic proteins which include enzymes; and regulatory proteins such as hormones. There are approximately 50,000 to 200,000 different proteins present in the human body, performing vital roles such as oxygen transport, muscle movement, immune defense, and metabolic processes.
Protien structure and Methods of protein structure determination Rajesh Kumar...
Protien structure and Methods of protein structure determination Rajesh Kumar...RajeshKumarKushwaha5
This document provides an overview of methods for determining protein structure, including X-ray crystallography, nuclear magnetic resonance, and cryo-electron microscopy. It discusses how X-ray crystallography involves growing protein crystals and bombarding them with X-rays to generate diffraction patterns used to build 3D electron density maps. Nuclear magnetic resonance measures distances between atomic nuclei by analyzing signals from atomic spins in magnetic fields. Cryo-electron microscopy images flash-frozen protein samples to determine structure at near-atomic resolution.PROTEINS.pptx
This document discusses proteins, including their definition, structure, classification, and roles in the body. It begins by defining proteins as complex molecules composed of amino acids joined by peptide bonds. It then discusses protein structure, including primary, secondary, tertiary, and quaternary levels. Proteins are classified based on solubility, composition, function, shape, and size. They play many important roles such as enzymatic catalysis, regulation, protection, storage, transport, structure, and contraction. The document provides a detailed overview of the nature and importance of proteins.
Protein- An Essential element
In this video the viewers will come to know about Proteins that is one of the ESSENTIAL COMPONENT in plant and animal. A protein is a complex, high molecular weight organic compound that consists of amino acids joined by peptide bonds. Here the Definition, meaning, configuration, nature, role and structure of proteins has been discussed in brief.
Portion explained:
1. Definition of proteins
2. Word Meaning of Protein
3. Sources of Protein
4. Configuration of Protein
6. Essential Amino Acids
7. Structural details of Protein
8. Nature of Protein
9. Role of protein in body
Protein bph
Proteins are organic macromolecules made of amino acids linked by peptide bonds. They range widely in size and function. The fundamental units are 20 different amino acids that make up the primary structure in different sequences. Secondary structures like alpha helices and beta sheets form due to hydrogen bonding of amino acid R groups. Tertiary and quaternary structures arise from further folding and interactions between polypeptide subunits. Proteins have important roles like enzymatic catalysis, transport, structure, regulation and defense. They are classified based on solubility and presence of non-protein groups.
Structure, functions and folding problems of protein
This document provides an overview of protein structure and folding. It discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. Common secondary structures like alpha helices and beta sheets are described. The document also introduces concepts like the Ramachandran plot, which maps allowed phi and psi dihedral angles in protein backbones. Protein folding and factors involved like molecular chaperones are also summarized. Disorders resulting from changes in protein conformation are briefly mentioned.
Chapter 6 protein and amino acids
protein metabolism
https://www.facebook.com/pages/%D8%A7%D9%84%D8%B9%D9%84%D8%A7%D8%AC-%D8%A7%D9%84%D9%85%D8%B5%D8%B1%D9%8A-%D9%84%D9%81%D9%8A%D8%B1%D9%88%D8%B3-%D8%B3%D9%89-%D9%88%D8%A7%D9%84%D8%A7%D9%8A%D8%AF%D8%B2/239710159549535
Core 6.1 and Option D1-D3
The document summarizes key aspects of human digestion and nutrition. It describes the main stages of digestion that occur in the oral cavity, stomach, small intestine and large intestine. Key points include:
- Digestion involves both physical and chemical breakdown of food facilitated by enzymes and accessory organs like the liver and pancreas.
- The small intestine is the primary site of nutrient absorption into the bloodstream through processes like diffusion, facilitated diffusion and active transport.
- The liver plays an important role in regulating blood composition and nutrient storage/processing through functions like detoxification, bile production, and albumin synthesis.
- A balanced diet with essential nutrients is important for human health, and macronutrients like carbohydrates
MACROMOLECULES-2023.pptx
This document provides information about macromolecules and their structure and function. It begins by stating the learning objectives of determining the structure and functions of biomolecules. It then defines macromolecules as large organic compounds formed from monomers joining together to create polymers. The four main types of macromolecules - carbohydrates, lipids, proteins, and nucleic acids - are introduced along with their monomer and polymer subunits. Specific examples and functions of each macromolecule type are then described in more detail over several pages.
cell revision.pptx
The document describes the key components and structures of animal cells. It discusses the constituents of cells, including water, ions, proteins, lipids and carbohydrates. It then describes the main organelles found in animal cells, including the nucleus, cytoplasm, cell membrane, mitochondria, endoplasmic reticulum, Golgi bodies, lysosomes and peroxisomes. It explains the functions of these organelles and how they work together to keep the cell alive.
protein and peptide dds.pptx
The document discusses protein and peptide drug delivery systems. It notes that proteins and peptides are degraded in the gastrointestinal tract but oral delivery is preferred over parenteral routes. Various pharmaceutical approaches can be used to overcome degradation and enhance oral absorption, including chemical modification, enzyme inhibitors, penetration enhancers, formulation vehicles, and mucoadhesive polymeric systems. Common protein and peptide drugs are discussed that are used for conditions like heart disease, diabetes, and infertility.
BCM3121_Lecture 1_2023.ppt
The document discusses protein biochemistry and includes the following information:
- It provides contact information for the lecturer, Dr. Burger, and class representatives. It also lists test dates for the semester.
- It defines biochemistry as the study of chemical processes in living organisms and notes that proteins are essential biomolecules involved in most biological functions.
- It explains that genes direct protein production through transcription and translation, and that amino acids are the building blocks of proteins. Each amino acid sequence is determined by the DNA sequence.
week 1 PHS 302 2022.pptx
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.
Similar to protein.pptx-Biochemistry (20)
Lec.3protein chem.classification new microsoft powerpoint presentation
Lec.3protein chem.classification new microsoft powerpoint presentation
Protien structure and Methods of protein structure determination Rajesh Kumar...
Protien structure and Methods of protein structure determination Rajesh Kumar...
Structure, functions and folding problems of protein
Structure, functions and folding problems of protein
More from ABHIJIT BHOYAR
Group Dynamic(presentation for nursing management)
Group dynamics is a system of behaviors and psychological processes occurring within a social group (intragroup dynamics), or between social groups (intergroup dynamics)
Discipline. pptx (Nursing management) nursing
the practice of training people to obey rules and behave well.
the practice of training your mind and body so that you control your actions and obey rules; a way of doing this
Diagnostic importance of enzymes.pptx
1. Enzymes like ALT, AST, ALP, GGT, CK, troponins, and PSA are used as biomarkers to diagnose diseases of the liver, heart, bones, muscles, and prostate.
2. Elevated levels of the liver enzymes ALT, AST, ALP, and GGT indicate potential liver damage or disease.
3. CK and troponin levels are measured to diagnose heart attacks, while high PSA levels may indicate prostate cancer.
Isoenzyme.pptx
Isoenzymes (or isozymes) are a group of enzymes that catalyze the same reaction but have different enzyme forms and catalytic efficiencies. Isozymes are usually distinguished by their electrophoretic mobilities.
Enzymes.pptx
An enzyme is a biological catalyst and is almost always a protein. It speeds up the rate of a specific chemical reaction in the cell. The enzyme is not destroyed during the reaction and is used over and over.
Atherosclerosis. pptx
atherosclerosis is the buildup of fats, cholesterol and other substances in and on the artery walls. This buildup is called plaque.
Lipoproteins & Lipid Profile .pptx
A complete cholesterol test — also called a lipid panel or lipid profile — is a blood test that can measure the amount of cholesterol and triglycerides in your blood
Ketone Bodies.pptx
Ketone bodies are produced by the liver and used peripherally as an energy source when glucose is not readily available.
Cholesterol.pptx
Cholesterol is a waxy substance found in your blood. Your body needs cholesterol to build healthy cells, but high levels of cholesterol can increase your risk of heart disease.
LIPIDS- Metabolism of Lipids.pptx
Lipid metabolism entails the oxidation of fatty acids to either generate energy or synthesize new lipids from smaller constituent molecules. Lipid metabolism is associated with carbohydrate metabolism,
LIPIDS-Digestion and absorption of Lipids.pptx
The digestion of lipids begins in the oral cavity through exposure to lingual lipases, which are secreted by glands in the tongue to begin the process of digesting triglycerides.
Lipids Classification, Essential.pptx
The term essential fatty acids (EFA) refers to those polyunsaturated fatty acids (PUFA) that must be provided by foods because these cannot be synthesized in the body yet are necessary for health
2. LIPIDS (Fatty Acids).pptx
Fatty acids are the building blocks of the fat in our bodies and in the food we eat. During digestion, the body breaks down fats into fatty acids, which can then be absorbed into the blood. Fatty acid molecules are usually joined together in groups of three, forming a molecule called a triglyceride.
lipids, Def. Classification, Function.pptx
The document defines lipids and classifies them. It discusses that lipids are a diverse group of organic compounds that are hydrophobic and insoluble in water. Lipids serve important functions like energy storage, cellular structure, signaling and energy transport. Lipids are classified as simple lipids, complex lipids, derived lipids and miscellaneous lipids. Simple lipids include fats, oils and waxes. Complex lipids contain additional groups like phosphate, carbohydrates or proteins. The document provides examples and descriptions of different lipid classes.
UTERUS_Nursing.pptx
Once the egg has left the ovary it can be fertilized and implant itself in the lining of the uterus. The main function of the uterus is to nourish the developing fetus prior to birth.
Kidney_Nursing.pptx
he kidneys are a vital organ critical to the human body. From filtering waste from blood to produce red blood cells, it serves a crucial role. With cells and tissue that work together in synchronized form for common function
Liver_Nursing.pptx
The liver is the largest solid organ located in the upper right abdomen. It performs hundreds of vital functions including removing toxins from the blood, maintaining blood sugar levels, and regulating blood clotting. The liver receives 20% of its blood supply from the hepatic artery and 80% from the portal vein. It is divided into four lobes and has five surfaces. The liver plays a crucial role in metabolism and detoxification.
Pancreas_Nursing.pptx
If you like share this PPT presentation to nursing students. The pancreas is an organ and a gland. Glands are organs that produce and release substances in the body. The pancreas performs two main functions: Exocrine function: Produces substances (enzymes) that help with digestion.
Spleen.pptx
he spleen is a fist-sized organ found in the upper left side of your abdomen, next to your stomach and behind your left ribs. It's an important part of your immune system but you can survive without it. This is because the liver can take over many of the spleen's functions
Popliteal Fossa.pptx
The Popliteal Fossa is a diamond-shaped space behind the knee joint. It is formed between the muscles in the posterior compartments of the thigh and leg. This anatomical landmark is the major route by which structures pass between the thigh and leg.
More from ABHIJIT BHOYAR (20)
Group Dynamic(presentation for nursing management)
Group Dynamic(presentation for nursing management)
Recently uploaded
Pollock and Snow "DEIA in the Scholarly Landscape, Session One: Setting Expec...
Pollock and Snow "DEIA in the Scholarly Landscape, Session One: Setting Expec...National Information Standards Organization (NISO)
This presentation was provided by Steph Pollock of The American Psychological Association’s Journals Program, and Damita Snow, of The American Society of Civil Engineers (ASCE), for the initial session of NISO's 2024 Training Series "DEIA in the Scholarly Landscape." Session One: 'Setting Expectations: a DEIA Primer,' was held June 6, 2024.The Diamonds of 2023-2024 in the IGRA collection
A review of the growth of the Israel Genealogy Research Association Database Collection for the last 12 months. Our collection is now passed the 3 million mark and still growing. See which archives have contributed the most. See the different types of records we have, and which years have had records added. You can also see what we have for the future.
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.
Leveraging Generative AI to Drive Nonprofit Innovation
In this webinar, participants learned how to utilize Generative AI to streamline operations and elevate member engagement. Amazon Web Service experts provided a customer specific use cases and dived into low/no-code tools that are quick and easy to deploy through Amazon Web Service (AWS.)
South African Journal of Science: Writing with integrity workshop (2024)
South African Journal of Science: Writing with integrity workshop (2024)Academy of Science of South Africa
A workshop hosted by the South African Journal of Science aimed at postgraduate students and early career researchers with little or no experience in writing and publishing journal articles.The History of Stoke Newington Street Names
Presented at the Stoke Newington Literary Festival on 9th June 2024
www.StokeNewingtonHistory.com
Wound healing PPT
This document provides an overview of wound healing, its functions, stages, mechanisms, factors affecting it, and complications.
A wound is a break in the integrity of the skin or tissues, which may be associated with disruption of the structure and function.
Healing is the body’s response to injury in an attempt to restore normal structure and functions.
Healing can occur in two ways: Regeneration and Repair
There are 4 phases of wound healing: hemostasis, inflammation, proliferation, and remodeling. This document also describes the mechanism of wound healing. Factors that affect healing include infection, uncontrolled diabetes, poor nutrition, age, anemia, the presence of foreign bodies, etc.
Complications of wound healing like infection, hyperpigmentation of scar, contractures, and keloid formation.
How to Create a More Engaging and Human Online Learning Experience
How to Create a More Engaging and Human Online Learning Experience Wahiba Chair Training & Consulting
Wahiba Chair's Talk at the 2024 Learning Ideas Conference. Reimagining Your Library Space: How to Increase the Vibes in Your Library No ...
Librarians are leading the way in creating future-ready citizens – now we need to update our spaces to match. In this session, attendees will get inspiration for transforming their library spaces. You’ll learn how to survey students and patrons, create a focus group, and use design thinking to brainstorm ideas for your space. We’ll discuss budget friendly ways to change your space as well as how to find funding. No matter where you’re at, you’ll find ideas for reimagining your space in this session.
How to Manage Your Lost Opportunities in Odoo 17 CRM
Odoo 17 CRM allows us to track why we lose sales opportunities with "Lost Reasons." This helps analyze our sales process and identify areas for improvement. Here's how to configure lost reasons in Odoo 17 CRM
How to Fix the Import Error in the Odoo 17
An import error occurs when a program fails to import a module or library, disrupting its execution. In languages like Python, this issue arises when the specified module cannot be found or accessed, hindering the program's functionality. Resolving import errors is crucial for maintaining smooth software operation and uninterrupted development processes.
BBR 2024 Summer Sessions Interview Training
Qualitative research interview training by Professor Katrina Pritchard and Dr Helen Williams
বাংলাদেশ অর্থনৈতিক সমীক্ষা (Economic Review) ২০২৪ UJS App.pdf
বাংলাদেশের অর্থনৈতিক সমীক্ষা ২০২৪ [Bangladesh Economic Review 2024 Bangla.pdf] কম্পিউটার , ট্যাব ও স্মার্ট ফোন ভার্সন সহ সম্পূর্ণ বাংলা ই-বুক বা pdf বই " সুচিপত্র ...বুকমার্ক মেনু 🔖 ও হাইপার লিংক মেনু 📝👆 যুক্ত ..
আমাদের সবার জন্য খুব খুব গুরুত্বপূর্ণ একটি বই ..বিসিএস, ব্যাংক, ইউনিভার্সিটি ভর্তি ও যে কোন প্রতিযোগিতা মূলক পরীক্ষার জন্য এর খুব ইম্পরট্যান্ট একটি বিষয় ...তাছাড়া বাংলাদেশের সাম্প্রতিক যে কোন ডাটা বা তথ্য এই বইতে পাবেন ...
তাই একজন নাগরিক হিসাবে এই তথ্য গুলো আপনার জানা প্রয়োজন ...।
বিসিএস ও ব্যাংক এর লিখিত পরীক্ষা ...+এছাড়া মাধ্যমিক ও উচ্চমাধ্যমিকের স্টুডেন্টদের জন্য অনেক কাজে আসবে ...
Hindi varnamala | hindi alphabet PPT.pdf
हिंदी वर्णमाला पीपीटी, hindi alphabet PPT presentation, hindi varnamala PPT, Hindi Varnamala pdf, हिंदी स्वर, हिंदी व्यंजन, sikhiye hindi varnmala, dr. mulla adam ali, hindi language and literature, hindi alphabet with drawing, hindi alphabet pdf, hindi varnamala for childrens, hindi language, hindi varnamala practice for kids, https://www.drmullaadamali.com
Recently uploaded (20)
Pollock and Snow "DEIA in the Scholarly Landscape, Session One: Setting Expec...
Pollock and Snow "DEIA in the Scholarly Landscape, Session One: Setting Expec...
spot a liar (Haiqa 146).pptx Technical writhing and presentation skills
spot a liar (Haiqa 146).pptx Technical writhing and presentation skills
Leveraging Generative AI to Drive Nonprofit Innovation
Leveraging Generative AI to Drive Nonprofit Innovation
South African Journal of Science: Writing with integrity workshop (2024)
South African Journal of Science: Writing with integrity workshop (2024)
How to Create a More Engaging and Human Online Learning Experience
How to Create a More Engaging and Human Online Learning Experience
Liberal Approach to the Study of Indian Politics.pdf
Liberal Approach to the Study of Indian Politics.pdf
Reimagining Your Library Space: How to Increase the Vibes in Your Library No ...
Reimagining Your Library Space: How to Increase the Vibes in Your Library No ...
How to Manage Your Lost Opportunities in Odoo 17 CRM
How to Manage Your Lost Opportunities in Odoo 17 CRM
বাংলাদেশ অর্থনৈতিক সমীক্ষা (Economic Review) ২০২৪ UJS App.pdf
বাংলাদেশ অর্থনৈতিক সমীক্ষা (Economic Review) ২০২৪ UJS App.pdf
protein.pptx-Biochemistry
- 1. PROTEIN
- 2. Specific Learning Objectives At the end of the lecture, student should be able to: 1. State meaning of protein 2. Difference in protein in peptides 3. Explain function of protein 4. Describe structure of protein 5. Explain properties of protein 6. Explain denaturation
- 3. Introduction • Proteins are organic compound of the living system containing C,H,O,N,P,S • Major function -it is a fundamental basis of structure and function of cell • Protein found in nail, skin, hair • Protein are polymer of amino acids • Made up of amino acid (building block)
- 4. What Are Proteins? • Large molecules • Made up of chains of amino acids • Are found in every cell in the body • Are involved in most of the body’s functions and life processes • The sequence of amino acids is determined by DNA
- 7. Biological important peptides • Glutathione • Thyrotropin releasing hormone • Oxytocin • Vasopressin (antidiuretic hormone, ADH • Angiotensin
- 9. FUNCTION Structural function- • collagen elastin found in bone matrix, vascular system and other organs • keratin present in epidermal tissues Dynamic function • All enzymes are protein • Hormones made up of protein • Help in transport • Defends against pathogens • Help in blood clotting
- 10. Structure of the Protein Primary structure Secondary structure Tertiary structure Quaternary structure Any alteration in the structure or sequencing changes the shape and function of the protein Four levels of structure 1 2 3 4
- 12. a) Primary Structure -INSULIN b) Secondary structure-MYOGLOBIN c) Tertiary structure- the overall three-dimensional arrangement of its polypeptide chain in space. d) Quaternary structure -HAEMOGLOBIN
- 13. Properties of protein • Protein exist as colloids in solution • The protein vary in their molecular wt • Wide variation in the shape • Precipitation of protein • Denaturation of protein
- 14. Denaturing • Alteration of the protein ’s shape and thus functions through the use of • Heat • Acids • Bases • Salts • Mechanical agitation • Primary structure is unchanged by denaturing
- 15. Denaturing a Protein Figure 6.5
- 17. Digestion and absorption of protein • Dietary proteins are of plant and animal origin Stages of protein digestion 1. Digestion by gastric juice-HCL, pepsin, rennin 2. Digestion by pancreatic juice- 5 proteases-trypsin, chymotrypsin, elastage, carboxypeptidase A and B 3. Digestion by intestinal juice- Enterokinase, Aminopeptidase, Dipeptidase
- 18. Protein Digestion: Part 1
- 19. Protein Digestion: Part 2
- 20. Protein Digestion: Part 3
- 21. ABSORPTION • Distal Jejunum • Ileum of small intestine
- 24. Expected Question Essay/ Situation Question • Explain protein with reference to definition, structure, classification and its functions. Short Question • Explain function of protein • Describe primary and secondary structure of protein • Explain properties of protein • Explain denaturation
- 25. References • Jacob Anthikad, Biochemistry for nurses • Pankaja Naik, Essentials of Biochemistry • Satyanarayan, Essentials of Biochemistry • A. C. Deb, Biochemistry
- 26. THANK YOU