Nucleotides are the basic building blocks of nucleic acids like DNA and RNA. They consist of three components: a nitrogenous base, a pentose sugar, and a phosphate group. The nitrogenous bases include purines like adenine and guanine, and pyrimidines like cytosine and thymine in DNA or uracil in RNA. The pentose sugars are either deoxyribose in DNA or ribose in RNA. Successive nucleotides are linked by phosphodiester bonds between the phosphate group of one nucleotide and the hydroxyl group of the next. This forms the hydrophilic backbone of nucleic acids and gives them polarity with distinct 5' and 3' ends. The specific hydrogen bonding between nucleotide base pairs
- Amino acids are the building blocks of proteins. The 20 common amino acids contain different functional groups like carboxylic acids, amines, and alcohols.
- At physiological pH, amino acids exist as zwitterions with both a positive and negative charge. They can behave as both acids and bases.
- The isoelectric point is the pH at which the amino acid has no net charge as it exists predominantly in its zwitterionic form. Titration curves can be used to determine the pKa values and isoelectric point of an amino acid.
Nucleotide Biosynthesis involves 2 processes. one is Denovo synthesis and other is Salvage pathway. An outline of both the processes has given in this presentation.
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.
The tricarboxylic acid (TCA) cycle is a series of enzyme-catalyzed reactions that forms a key part of aerobic respiration in cells. It was discovered by Hans Krebs in 1937 and is also known as the Krebs cycle or citric acid cycle. The cycle occupies a central position in metabolism, using acetate to generate carbon dioxide, reducing agents like NADH, and ATP through oxidative phosphorylation. It provides precursors for amino acid and nucleotide biosynthesis. The cycle is critical for generating the majority of a cell's energy needs through the complete oxidation of carbohydrates, fatty acids, and amino acids.
There are 20 common amino acids that serve as the building blocks of proteins. Amino acids contain an amino group, a carboxyl group, and a variable side chain. They join together through peptide bonds to form polypeptides and proteins. Ten of the 20 amino acids are considered essential and must be obtained through diet as humans cannot synthesize them. Proteins perform a wide variety of important functions in the body.
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.
This document discusses the chemistry of proteins and amino acids. It begins by explaining that proteins are abundant organic molecules that make up 50% of cellular mass and are essential for structure and function. The document then goes into detail about the classification, structure, properties and roles of the 20 standard amino acids that make up proteins. It describes how amino acids combine through peptide bonds to form polypeptide chains and proteins. The document provides a comprehensive overview of the biochemistry of proteins and amino acids.
Nucleotides are the basic building blocks of nucleic acids like DNA and RNA. They consist of three components: a nitrogenous base, a pentose sugar, and a phosphate group. The nitrogenous bases include purines like adenine and guanine, and pyrimidines like cytosine and thymine in DNA or uracil in RNA. The pentose sugars are either deoxyribose in DNA or ribose in RNA. Successive nucleotides are linked by phosphodiester bonds between the phosphate group of one nucleotide and the hydroxyl group of the next. This forms the hydrophilic backbone of nucleic acids and gives them polarity with distinct 5' and 3' ends. The specific hydrogen bonding between nucleotide base pairs
- Amino acids are the building blocks of proteins. The 20 common amino acids contain different functional groups like carboxylic acids, amines, and alcohols.
- At physiological pH, amino acids exist as zwitterions with both a positive and negative charge. They can behave as both acids and bases.
- The isoelectric point is the pH at which the amino acid has no net charge as it exists predominantly in its zwitterionic form. Titration curves can be used to determine the pKa values and isoelectric point of an amino acid.
Nucleotide Biosynthesis involves 2 processes. one is Denovo synthesis and other is Salvage pathway. An outline of both the processes has given in this presentation.
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.
The tricarboxylic acid (TCA) cycle is a series of enzyme-catalyzed reactions that forms a key part of aerobic respiration in cells. It was discovered by Hans Krebs in 1937 and is also known as the Krebs cycle or citric acid cycle. The cycle occupies a central position in metabolism, using acetate to generate carbon dioxide, reducing agents like NADH, and ATP through oxidative phosphorylation. It provides precursors for amino acid and nucleotide biosynthesis. The cycle is critical for generating the majority of a cell's energy needs through the complete oxidation of carbohydrates, fatty acids, and amino acids.
There are 20 common amino acids that serve as the building blocks of proteins. Amino acids contain an amino group, a carboxyl group, and a variable side chain. They join together through peptide bonds to form polypeptides and proteins. Ten of the 20 amino acids are considered essential and must be obtained through diet as humans cannot synthesize them. Proteins perform a wide variety of important functions in the body.
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.
This document discusses the chemistry of proteins and amino acids. It begins by explaining that proteins are abundant organic molecules that make up 50% of cellular mass and are essential for structure and function. The document then goes into detail about the classification, structure, properties and roles of the 20 standard amino acids that make up proteins. It describes how amino acids combine through peptide bonds to form polypeptide chains and proteins. The document provides a comprehensive overview of the biochemistry of proteins and amino acids.
The document provides information about amino acids and their classification. It discusses that amino acids are the monomer units that make up protein polymers. They can be classified based on their structure, side chains, nutritional requirements, and metabolic fate. The 20 standard amino acids are discussed in detail, including their physical and chemical properties. Key reactions of amino acids involving their amino, carboxyl, and side chain groups are also summarized.
1. Glycogenesis is the process of glycogen synthesis, the storage form of carbohydrates in animals and plants.
2. Glycogen is synthesized from glucose-1-phosphate through the addition of glucose units via alpha-1,4 glycosidic bonds and branching via alpha-1,6 bonds, forming a branched polymer structure.
3. Glycogenesis occurs primarily in the liver and muscles, with liver glycogen functioning to regulate blood glucose levels between meals through glycogenolysis and export of glucose, while muscle glycogen provides glucose for local glycolysis.
Proteins are the macromolecules responsible for the biological processes in the cell. They consist at their most basic level of a chain of amino acids, determined by the sequence of nucleotides in a gene. Depending on the amino acid sequence (different amino acids have different biochemical properties) and interactions with their environment, proteins fold into a three-dimensional structure, which allows them to interact with other proteins and molecules and perform their function
Enzymes definitions, types & classificationJasmineJuliet
Enzyme - Introduction, Biocatalysts, Definition of enzymes, Types of enzymes, classification of enzyme, Nomenclature of enzymes, EC number, Types of enzymes with examples, and reaction.
The document provides information on amino acids including their history, classification, structure and properties. It discusses how amino acids were first discovered in 1806 and classified based on nutritional requirements, polarity, metabolic fate and structure. Key points include that amino acids have an amino group and carboxyl group, exist in ionized forms in biological systems, and 20 are used as building blocks of proteins. Their physical properties like solubility, isoelectric point and ability to act as ampholytes are also covered.
The slide has some brief introduction to nucleotide chemistry, History, General features of nucleotides, Nomenclature, Individual properties of bases, Classification
and Synthetic analogues of biomedical importance.
The electron transport chain (ETC) is a series of protein complexes and carriers in the inner mitochondrial membrane that transport electrons from electron donors like NADH to final acceptors like oxygen. This transports protons from the mitochondrial matrix to the intermembrane space, building up a proton gradient. ATP synthase uses this proton gradient to phosphorylate ADP, producing approximately 34 ATP per glucose. The ETC is crucial for aerobic respiration as it extracts much more energy than glycolysis and the Krebs cycle alone.
L-amino acids are the monomer units that make up the polypeptide chains of proteins. Short amino acid polymers called peptides also play important roles as hormones, hormone-releasing factors, neuromodulators, or neurotransmitters. There are 20 standard amino acids that are the basic building blocks of proteins in the human body. Amino acids can be classified in different ways, including by their structure, side chain properties, nutritional requirements, and metabolic fate.
The document summarizes amino acid biosynthesis in mammals. It discusses the different families of amino acids and how they are synthesized from common precursors like glutamate. It describes regulation of biosynthesis through feedback inhibition. Finally, it outlines some genetic diseases that result from defects in amino acid metabolism, like phenylketonuria and homocystinuria.
Purines and pyrimidines are heterocyclic nitrogen-containing compounds that are major components of nucleotides, which build DNA and RNA. They function as building blocks of nucleic acids and are involved in various cellular processes as components of coenzymes and metabolic regulators. Nucleotides are synthesized through both de novo and salvage pathways. The de novo synthesis of purines involves multiple steps utilizing various substrates and is regulated at several points to control nucleotide levels. IMP is an early intermediate that is converted to AMP and GMP through reciprocal regulation. Purine degradation yields uric acid, while ingested nucleic acids undergo digestion and absorption as nucleosides and bases to contribute to nucleotide synthesis.
The synthesis of glycogen from glucose (glycogenesis) involves multiple enzymatic steps that takes place in the cytosol. Glucose is first converted to glucose-6-phosphate by hexokinase or glucokinase in muscle and liver respectively. It is then converted to UDP-glucose which acts as the donor of glucose units. A glycogen primer, initiated by the enzyme glycogen synthase, is required to begin glycogen synthesis. Glycogen is then elongated through alpha-1,4 glycosidic linkages by glycogen synthase and branched through alpha-1,6 linkages by the branching enzyme glucosyltransferase. This leads to the formation of the branched glyc
This document provides information about glycolysis, including:
1) Glycolysis involves the breakdown of glucose into pyruvate, producing 2 ATP and 2 NADH. There are 10 enzyme-catalyzed reactions in two stages.
2) Key regulatory enzymes include hexokinase, phosphofructokinase, and pyruvate kinase which control the flux of glycolysis.
3) Under anaerobic conditions, NADH is regenerated through lactic acid or ethanol fermentation to allow glycolysis to continue.
Gives in detail primary, secondary, tertiary and Quaternary structure of proteins. Gives classification of secondary structure: alpha helix, beta pleated sheet and different types of tight turns and explains most commonly found tight turn in proteins i.e. beta turn. Briefs about the Ramachandran plot of proteins, dihedral or torsion angles and explains why glycine and proline act as alpha helix breakers. Explains tertiary structure of proteins and different covalent and non covalent bonds in the tertiary structure and relative importance of these bonding interactions. Details about the quaternary structure of proteins and explains why hemoglobin is a quaternary protein and insulin is not.
The document discusses the tricarboxylic acid (TCA) cycle, also known as the Krebs cycle or citric acid cycle. It provides three key points:
1. The TCA cycle is the final common pathway for the oxidation of carbohydrates, fats, and proteins to produce energy in the form of ATP. It involves the oxidation of acetyl-CoA to carbon dioxide and generates reduced cofactors NADH and FADH2 that feed into the electron transport chain.
2. The cycle occurs in the mitochondrial matrix and is tightly regulated. It generates 3 NADH and 1 FADH2 per acetyl-CoA molecule oxidized, which can ultimately produce around 12 ATP
The TCA cycle, also known as the Krebs cycle or citric acid cycle, is the central metabolic pathway that catalyzes the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins to produce carbon dioxide, water, and energy in the form of ATP, NADH, and FADH2. The TCA cycle occurs in the mitochondrial matrix and is the final common pathway for the oxidation of these three macronutrient types. Through a series of chemical reactions, acetyl-CoA is oxidized, producing carbon dioxide and hydrogen ions that will be used in the electron transport chain to generate ATP through oxidative phosphorylation.
Proteins are macromolecules composed of amino acid subunits linked by peptide bonds. There are 20 common amino acids that make up proteins. Amino acids are classified based on properties like charge, polarity, and essentiality. Proteins form through peptide bond formation between amino acid residues, resulting in primary, secondary, tertiary, and quaternary structure levels that determine a protein's shape and function.
The document summarizes palmitate synthesis from acetyl-CoA and malonyl-CoA. Specifically, it notes that palmitate synthesis requires 8 acetyl-CoA molecules, 7 ATP molecules, 14 NADPH molecules, and 14 hydrogen ions to produce palmitate, 8 CoA molecules, 7 ADP molecules, 7 phosphate ions, and 6 water molecules. It further explains that in palmitate, only 2 carbon atoms come from acetyl-CoA, while the remaining 14 carbon atoms are from malonyl-CoA, which is produced from acetyl-CoA.
1. The document summarizes purine nucleotide synthesis, which involves multiple enzymatic reactions using substrates like aspartate, glutamine, glycine, and CO2 to build the purine ring structure on ribose 5-phosphate.
2. Liver is the major site of de novo purine synthesis, while erythrocytes and brain must salvage purines due to their inability to synthesize them.
3. Feedback inhibition regulates purine synthesis at committed steps, and analogs like 6-mercaptopurine can inhibit pathways leading to AMP and GMP formation.
1. Nucleotides consist of a nitrogenous base, sugar (ribose or deoxyribose), and phosphate. Purines and pyrimidines are synthesized via de novo or salvage pathways to form nucleotides.
2. Purine synthesis occurs in multiple steps starting from PRPP, with the purine ring built step-by-step. Pyrimidine synthesis involves first forming the pyrimidine ring and then attaching it to ribose-5-phosphate.
3. Errors in purine synthesis can cause diseases like gout, which results from excess uric acid in the blood due to defects in purine metabolism or uric acid excretion. Several drugs target purine synthesis
1) Amino acids are the building blocks of proteins and are linked together by peptide bonds to form polypeptides or proteins.
2) There are 20 common amino acids that occur in proteins. Amino acids have an amino group, carboxyl group, hydrogen atom, and variable side chain.
3) Proteins have a primary structure defined by the sequence of amino acids, and higher order structures including secondary structures like alpha helices and beta sheets formed by hydrogen bonding between amino acids.
Amino acids are the building blocks of proteins. There are over 300 amino acids found in nature but only 20 are used in protein construction. Amino acids contain an amino group, a carboxyl group, a hydrogen atom, and a variable side chain. They can be classified based on their chemical, physical, and nutritional properties. Amino acids link together via peptide bonds to form polypeptides and proteins. The difference between peptides and proteins is that peptides contain less than 50 amino acids while proteins contain 50 or more amino acids.
The document provides information about amino acids and their classification. It discusses that amino acids are the monomer units that make up protein polymers. They can be classified based on their structure, side chains, nutritional requirements, and metabolic fate. The 20 standard amino acids are discussed in detail, including their physical and chemical properties. Key reactions of amino acids involving their amino, carboxyl, and side chain groups are also summarized.
1. Glycogenesis is the process of glycogen synthesis, the storage form of carbohydrates in animals and plants.
2. Glycogen is synthesized from glucose-1-phosphate through the addition of glucose units via alpha-1,4 glycosidic bonds and branching via alpha-1,6 bonds, forming a branched polymer structure.
3. Glycogenesis occurs primarily in the liver and muscles, with liver glycogen functioning to regulate blood glucose levels between meals through glycogenolysis and export of glucose, while muscle glycogen provides glucose for local glycolysis.
Proteins are the macromolecules responsible for the biological processes in the cell. They consist at their most basic level of a chain of amino acids, determined by the sequence of nucleotides in a gene. Depending on the amino acid sequence (different amino acids have different biochemical properties) and interactions with their environment, proteins fold into a three-dimensional structure, which allows them to interact with other proteins and molecules and perform their function
Enzymes definitions, types & classificationJasmineJuliet
Enzyme - Introduction, Biocatalysts, Definition of enzymes, Types of enzymes, classification of enzyme, Nomenclature of enzymes, EC number, Types of enzymes with examples, and reaction.
The document provides information on amino acids including their history, classification, structure and properties. It discusses how amino acids were first discovered in 1806 and classified based on nutritional requirements, polarity, metabolic fate and structure. Key points include that amino acids have an amino group and carboxyl group, exist in ionized forms in biological systems, and 20 are used as building blocks of proteins. Their physical properties like solubility, isoelectric point and ability to act as ampholytes are also covered.
The slide has some brief introduction to nucleotide chemistry, History, General features of nucleotides, Nomenclature, Individual properties of bases, Classification
and Synthetic analogues of biomedical importance.
The electron transport chain (ETC) is a series of protein complexes and carriers in the inner mitochondrial membrane that transport electrons from electron donors like NADH to final acceptors like oxygen. This transports protons from the mitochondrial matrix to the intermembrane space, building up a proton gradient. ATP synthase uses this proton gradient to phosphorylate ADP, producing approximately 34 ATP per glucose. The ETC is crucial for aerobic respiration as it extracts much more energy than glycolysis and the Krebs cycle alone.
L-amino acids are the monomer units that make up the polypeptide chains of proteins. Short amino acid polymers called peptides also play important roles as hormones, hormone-releasing factors, neuromodulators, or neurotransmitters. There are 20 standard amino acids that are the basic building blocks of proteins in the human body. Amino acids can be classified in different ways, including by their structure, side chain properties, nutritional requirements, and metabolic fate.
The document summarizes amino acid biosynthesis in mammals. It discusses the different families of amino acids and how they are synthesized from common precursors like glutamate. It describes regulation of biosynthesis through feedback inhibition. Finally, it outlines some genetic diseases that result from defects in amino acid metabolism, like phenylketonuria and homocystinuria.
Purines and pyrimidines are heterocyclic nitrogen-containing compounds that are major components of nucleotides, which build DNA and RNA. They function as building blocks of nucleic acids and are involved in various cellular processes as components of coenzymes and metabolic regulators. Nucleotides are synthesized through both de novo and salvage pathways. The de novo synthesis of purines involves multiple steps utilizing various substrates and is regulated at several points to control nucleotide levels. IMP is an early intermediate that is converted to AMP and GMP through reciprocal regulation. Purine degradation yields uric acid, while ingested nucleic acids undergo digestion and absorption as nucleosides and bases to contribute to nucleotide synthesis.
The synthesis of glycogen from glucose (glycogenesis) involves multiple enzymatic steps that takes place in the cytosol. Glucose is first converted to glucose-6-phosphate by hexokinase or glucokinase in muscle and liver respectively. It is then converted to UDP-glucose which acts as the donor of glucose units. A glycogen primer, initiated by the enzyme glycogen synthase, is required to begin glycogen synthesis. Glycogen is then elongated through alpha-1,4 glycosidic linkages by glycogen synthase and branched through alpha-1,6 linkages by the branching enzyme glucosyltransferase. This leads to the formation of the branched glyc
This document provides information about glycolysis, including:
1) Glycolysis involves the breakdown of glucose into pyruvate, producing 2 ATP and 2 NADH. There are 10 enzyme-catalyzed reactions in two stages.
2) Key regulatory enzymes include hexokinase, phosphofructokinase, and pyruvate kinase which control the flux of glycolysis.
3) Under anaerobic conditions, NADH is regenerated through lactic acid or ethanol fermentation to allow glycolysis to continue.
Gives in detail primary, secondary, tertiary and Quaternary structure of proteins. Gives classification of secondary structure: alpha helix, beta pleated sheet and different types of tight turns and explains most commonly found tight turn in proteins i.e. beta turn. Briefs about the Ramachandran plot of proteins, dihedral or torsion angles and explains why glycine and proline act as alpha helix breakers. Explains tertiary structure of proteins and different covalent and non covalent bonds in the tertiary structure and relative importance of these bonding interactions. Details about the quaternary structure of proteins and explains why hemoglobin is a quaternary protein and insulin is not.
The document discusses the tricarboxylic acid (TCA) cycle, also known as the Krebs cycle or citric acid cycle. It provides three key points:
1. The TCA cycle is the final common pathway for the oxidation of carbohydrates, fats, and proteins to produce energy in the form of ATP. It involves the oxidation of acetyl-CoA to carbon dioxide and generates reduced cofactors NADH and FADH2 that feed into the electron transport chain.
2. The cycle occurs in the mitochondrial matrix and is tightly regulated. It generates 3 NADH and 1 FADH2 per acetyl-CoA molecule oxidized, which can ultimately produce around 12 ATP
The TCA cycle, also known as the Krebs cycle or citric acid cycle, is the central metabolic pathway that catalyzes the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins to produce carbon dioxide, water, and energy in the form of ATP, NADH, and FADH2. The TCA cycle occurs in the mitochondrial matrix and is the final common pathway for the oxidation of these three macronutrient types. Through a series of chemical reactions, acetyl-CoA is oxidized, producing carbon dioxide and hydrogen ions that will be used in the electron transport chain to generate ATP through oxidative phosphorylation.
Proteins are macromolecules composed of amino acid subunits linked by peptide bonds. There are 20 common amino acids that make up proteins. Amino acids are classified based on properties like charge, polarity, and essentiality. Proteins form through peptide bond formation between amino acid residues, resulting in primary, secondary, tertiary, and quaternary structure levels that determine a protein's shape and function.
The document summarizes palmitate synthesis from acetyl-CoA and malonyl-CoA. Specifically, it notes that palmitate synthesis requires 8 acetyl-CoA molecules, 7 ATP molecules, 14 NADPH molecules, and 14 hydrogen ions to produce palmitate, 8 CoA molecules, 7 ADP molecules, 7 phosphate ions, and 6 water molecules. It further explains that in palmitate, only 2 carbon atoms come from acetyl-CoA, while the remaining 14 carbon atoms are from malonyl-CoA, which is produced from acetyl-CoA.
1. The document summarizes purine nucleotide synthesis, which involves multiple enzymatic reactions using substrates like aspartate, glutamine, glycine, and CO2 to build the purine ring structure on ribose 5-phosphate.
2. Liver is the major site of de novo purine synthesis, while erythrocytes and brain must salvage purines due to their inability to synthesize them.
3. Feedback inhibition regulates purine synthesis at committed steps, and analogs like 6-mercaptopurine can inhibit pathways leading to AMP and GMP formation.
1. Nucleotides consist of a nitrogenous base, sugar (ribose or deoxyribose), and phosphate. Purines and pyrimidines are synthesized via de novo or salvage pathways to form nucleotides.
2. Purine synthesis occurs in multiple steps starting from PRPP, with the purine ring built step-by-step. Pyrimidine synthesis involves first forming the pyrimidine ring and then attaching it to ribose-5-phosphate.
3. Errors in purine synthesis can cause diseases like gout, which results from excess uric acid in the blood due to defects in purine metabolism or uric acid excretion. Several drugs target purine synthesis
1) Amino acids are the building blocks of proteins and are linked together by peptide bonds to form polypeptides or proteins.
2) There are 20 common amino acids that occur in proteins. Amino acids have an amino group, carboxyl group, hydrogen atom, and variable side chain.
3) Proteins have a primary structure defined by the sequence of amino acids, and higher order structures including secondary structures like alpha helices and beta sheets formed by hydrogen bonding between amino acids.
Amino acids are the building blocks of proteins. There are over 300 amino acids found in nature but only 20 are used in protein construction. Amino acids contain an amino group, a carboxyl group, a hydrogen atom, and a variable side chain. They can be classified based on their chemical, physical, and nutritional properties. Amino acids link together via peptide bonds to form polypeptides and proteins. The difference between peptides and proteins is that peptides contain less than 50 amino acids while proteins contain 50 or more amino acids.
Amino acids are the building blocks of proteins. There are 20 common amino acids that make up proteins through peptide bonds. Amino acids have four groups attached to the alpha carbon including an amino group, carboxyl group, hydrogen, and a variable side chain. Amino acids can be classified based on their structure and properties. Proteins have four levels of structure - primary, secondary, tertiary, and quaternary - which determine their shape and function.
The document discusses protein structure and function. It covers the following key points:
1) Amino acids are the building blocks of proteins. There are 20 common amino acids that make up proteins through peptide bond formation.
2) Protein structure is hierarchical, consisting of primary, secondary, tertiary, and sometimes quaternary levels. Secondary structure includes alpha helices and beta sheets formed by hydrogen bonding. Tertiary structure is determined by interactions between amino acid side chains.
3) Proteins are classified based on solubility, composition, and derivation. Simple proteins hydrolyze to amino acids, while conjugated proteins also contain non-protein components like lipids, sugars, or metals. Derived proteins result from
Amino acids structure classification & function by KK Sahu sirKAUSHAL SAHU
This document provides an overview of amino acids, including their structure, classification, properties, and functions. It discusses that amino acids are the building blocks of proteins and there are 20 common amino acids. They are classified based on the composition of their side chains, number of amino and carboxyl groups, and polarity. Key points covered include their amphoteric nature, ionization states, titration curves, essential vs. nonessential amino acids, and roles in biochemical pathways and protein structure.
Some reagents or conditions that can cause protein denaturation include:
- High or low pH (acids and bases)
- Heat
- Detergents
- Organic solvents (alcohol, acetone)
- Heavy metals (salts of heavy metals like copper, mercury)
- Radiation (UV light, X-rays)
The document discusses the structure and properties of proteins and amino acids. Some key points:
- Proteins are polymers of amino acids linked by peptide bonds. There are 20 standard amino acids that vary in properties based on their side chains.
- Proteins have primary, secondary, tertiary, and quaternary levels of structure determined by amino acid sequence and interactions.
- Amino acids form peptides and proteins through condensation reactions between carboxyl and amino groups, forming peptide bonds.
- Proteins can be classified based on function, shape, nutritional value, and composition. Structural proteins like collagen resist digestion while globular proteins are soluble.
The document discusses the basic structure and properties of amino acids. It begins by explaining that amino acids are the building blocks of proteins and there are 20 different amino acids used in protein synthesis. It then describes the common structure of amino acids, including the alpha carbon, amino group, carboxyl group, hydrogen, and variable side chain. The document proceeds to classify and discuss the properties of different amino acids, including their chemical properties, polarity, essential/nonessential status, and effects on metabolism. It concludes by listing the one-letter codes for the 20 standard amino acids used in proteins.
Proteins are polymers composed of amino acids linked by peptide bonds. They have a primary structure defined by the sequence of amino acids, and can form secondary structures like alpha helices and beta sheets through hydrogen bonding. The overall 3D shape of a protein formed by interactions between amino acid side chains is its tertiary structure. Some proteins are made of multiple subunits and have a quaternary structure defined by their arrangement. Protein structures determine their diverse functions in the body.
There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves hydrogen bonding between amino acids to form common structures like alpha helices and beta sheets. Tertiary structure describes the three-dimensional folding of the protein chain stabilized by interactions between R groups. Quaternary structure refers to complexes of multiple polypeptide subunits. Proteins are classified based on their structure, composition, and function. Fibrous, globular, and intermediate proteins are distinguished by their structure, while simple and conjugated proteins differ in whether they contain additional non-protein groups.
This presentation the chemical structure of natural amino acids. It also classifies amino acids according to several criteria e.g., structure (aliphatic, aromatic, and heterocyclic amino acids), reaction (Neutral, acidic and basic amino acids), polarity (polar and nonpolar amino acids), and metabolic fate ( glucogenic, ketogenic and glucoketogenic amino acids)
Amino acids are the building blocks of proteins. They contain an amine group, a carboxylic acid group, and a side chain specific to each amino acid. Amino acids can be classified based on their side chains as aliphatic, aromatic, acidic, etc. Amino acids are also classified as essential or non-essential based on whether the human body can synthesize them. Amino acids undergo various reactions like transamination, where the amino group is transferred from one amino acid to a keto acid. They are also broken down through oxidative deamination, where the amino group is removed and converted to ammonia.
Proteins are composed of amino acids and have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Common secondary structures include alpha helices and beta pleated sheets formed by hydrogen bonding. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Globular proteins fold such that hydrophobic residues are buried inside and hydrophilic residues face outward, while fibrous proteins form insoluble fibers.
The document discusses the structure, classification, and properties of amino acids. It begins by defining amino acids as organic compounds containing amino and carboxyl groups. There are 20 standard amino acids that make up mammalian proteins. These can be classified into groups based on their side chains. Amino acids are also classified as essential or non-essential based on whether the human body can synthesize them. Additionally, amino acids can be categorized as glycogenic, ketogenic, or both based on their role in glucose or fat synthesis. The document concludes by mentioning two recently discovered amino acids, selenocysteine and pyrrolysine.
Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up the proteins in living organisms. Amino acids contain an amino group and a carboxyl group, and can be joined together via peptide bonds to form polypeptide chains. Proteins have complex structures with four levels of organization - primary, secondary, tertiary, and quaternary structure. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structures include alpha helices and beta sheets formed from regular patterns of hydrogen bonds between amino acids in the chain.
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.
Proteins are polymers composed of amino acids joined by peptide bonds. There are 20 genetically encoded amino acids that vary in properties like polarity, charge, and solubility. Protein structure is organized in four levels - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence, which determines the higher order structures that influence a protein's function, such as enzyme catalysis or oxygen transport. Sanger's method uses 1-fluoro-2,4-dinitrobenzene to label the N-terminal amino acid and determine protein sequence.
This was a report regarding amino acids and peptides that was prepared by our group and this report made in order to make a score. Hope this slide makes more it to be on help.
This PPTX is a basic presentation of a short sight of 10 minutes, about what role, classification & properties of amino acids, Protein organization, functions of proteins
Debridement is an important component of the wound bed preparation (WBP) management Model.
Cause of the wound and patient-centered concerns, debridement is a necessary step in local wound care.
Debridement is the removal of necrotic tissue, exudate, bacteria, and metabolic waste from a wound in order to improve or facilitate the healing process
Chest pain or discomfort
Common presenting symptom of cardiovascular disease
May be cardiac or noncardiac in origin.
Cardiac – angina, MI, pericarditis, mitral valve prolapse, dissecting aortic aneurysm
Non cardiac – anemia (physical exertion), cervical disc disease, anxiety, trigger points etc
Follows pattern of ulnar nerve distribution (heart supplied by C3-T4 spinal segments)
Radiating pain to neck, jaw, upper trapezius, upper back, shoulder or arms (commonly left
This document provides an introduction to research methodology. It defines research as the pursuit of truth through study, observation, comparison and experimentation. Research can be motivated by a desire to validate intuition, improve methods, meet job demands, or pursue publication. The types of research covered include descriptive research, which reports on current phenomena; applied research, which aims to solve practical problems; and quantitative versus qualitative research. Key parts of the research process discussed are choosing a subject and objectives, developing hypotheses, collecting and analyzing data, making conclusions, and testing those conclusions.
Biologist & gerontologist used concept of senescence to explain biological aging
Senescence or normal aging refers to a gradual, time related to biological process that takes places as degenerative processes overtake regenerative or growth processes.
or
senescence: a change in the behavior of an organism with age leading to a decreased power of survival and adjustment
Immunology plays a very important role in homeostasis but it possesses two edge sword actions. Either hypo or hyperimmunity both can cause systemic diseases which will manifest in the oral cavity.
Immunomodulators are the agents which modulate the body immunity according to
the need.
There are natural and synthetic immunomodulatory agents .
Endocrinology is a specialty of medicine; some would say a sub-specialty of internal medicine, which deals with the diagnosis and treatment of diseases related to hormones. Endocrinology covers such human functions as the coordination of metabolism, respiration, reproduction, sensory perception, and movement
non-skeletal mesodermal tissues: adipose tissue, fibrous tissue, muscle, blood vessels and peripheral nerves (despite neuroectodermal origin)
benign, malignant and intermediate (low-grade malignant – locally aggressive, can recur, no metastatic potential)
originate from primitive mesenchymal stem cells
classification according to differentiation lines (e.g. liposarcoma is not a tumor arising from adipose tissue but exhibiting lipoblastic differentiation)
Down syndrome (DS or DNS), also known as trisomy 21, is a genetic disorder caused by the presence of all or part of a third copy of chromosome 21. It is typically associated with physical growth delays, characteristic facial features and mild to moderate intellectual disability. The average IQ of a young adult with Down syndrome is 50, equivalent to the mental ability of an 8- or 9-year-old child, but this can vary widely.
Facial pain is pain felt in any part of the face, including the mouth and eyes.
It’s normally due to an injury or a headache, occasionally facial pain may also be due to neurological or vascular causes, but equally well may be dental in origin.
The lymphatic system is responsible for the production, transport and filtration of lymph fluid throughout the body. In addition to its important circulatory functions, the lymphatic system also has important immunological functions
The pressure of the blood in the circulatory system, often measured for diagnosis since it is closely related to the force and rate of the heartbeat and the diameter and elasticity of the arterial walls.
Gastric secretion is produced by epithelial cells in the stomach's gastric glands. These cells include parietal cells, chief cells, mucus-secreting cells, and hormone-producing cells. Parietal cells secrete hydrochloric acid and intrinsic factor. Chief cells secrete pepsinogen, which is converted to the protease pepsin by hydrochloric acid. Mucus-secreting cells produce a bicarbonate-rich mucus that protects the stomach lining. Hormone-producing cells secrete gastrin, somatostatin, and histamine, which help regulate acid secretion.
Eating a diet high in vegetables, fruits, whole grains, and legumes.
Choosing lean, low-fat sources of protein.
Limiting sweets, soft drinks, and foods with added sugar.
Including proteins, carbohydrates, and a little good fat in all meals and snacks.
Vectors are organisms that transmit pathogens and parasites from one infected person (or animal) to another, causing serious diseases in human populations
This document provides an overview of key concepts in personality psychology, including definitions of personality, major perspectives on personality development, and approaches to personality assessment. It discusses Freud's psychoanalytic perspective and concepts like the id, ego, superego, and psychosexual stages. It also covers Maslow's hierarchy of needs and the importance of satisfying lower needs before progressing to higher needs. Finally, it describes common objective and projective personality tests, such as the MMPI, Rorschach, and TAT.
This document discusses memory, cognition, and thinking. It covers the stages of memory including encoding, storage and retrieval. It describes the different types of memory like sensory, short-term and long-term. It discusses theories of thinking such as creative, analytical and critical thinking. It also covers problem solving strategies and cognition. The goal is to understand memory, improve memory, understand thinking processes, and learn problem solving techniques.
Cell Therapy Expansion and Challenges in Autoimmune DiseaseHealth Advances
There is increasing confidence that cell therapies will soon play a role in the treatment of autoimmune disorders, but the extent of this impact remains to be seen. Early readouts on autologous CAR-Ts in lupus are encouraging, but manufacturing and cost limitations are likely to restrict access to highly refractory patients. Allogeneic CAR-Ts have the potential to broaden access to earlier lines of treatment due to their inherent cost benefits, however they will need to demonstrate comparable or improved efficacy to established modalities.
In addition to infrastructure and capacity constraints, CAR-Ts face a very different risk-benefit dynamic in autoimmune compared to oncology, highlighting the need for tolerable therapies with low adverse event risk. CAR-NK and Treg-based therapies are also being developed in certain autoimmune disorders and may demonstrate favorable safety profiles. Several novel non-cell therapies such as bispecific antibodies, nanobodies, and RNAi drugs, may also offer future alternative competitive solutions with variable value propositions.
Widespread adoption of cell therapies will not only require strong efficacy and safety data, but also adapted pricing and access strategies. At oncology-based price points, CAR-Ts are unlikely to achieve broad market access in autoimmune disorders, with eligible patient populations that are potentially orders of magnitude greater than the number of currently addressable cancer patients. Developers have made strides towards reducing cell therapy COGS while improving manufacturing efficiency, but payors will inevitably restrict access until more sustainable pricing is achieved.
Despite these headwinds, industry leaders and investors remain confident that cell therapies are poised to address significant unmet need in patients suffering from autoimmune disorders. However, the extent of this impact on the treatment landscape remains to be seen, as the industry rapidly approaches an inflection point.
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.
ABDOMINAL TRAUMA in pediatrics part one.drhasanrajab
Abdominal trauma in pediatrics refers to injuries or damage to the abdominal organs in children. It can occur due to various causes such as falls, motor vehicle accidents, sports-related injuries, and physical abuse. Children are more vulnerable to abdominal trauma due to their unique anatomical and physiological characteristics. Signs and symptoms include abdominal pain, tenderness, distension, vomiting, and signs of shock. Diagnosis involves physical examination, imaging studies, and laboratory tests. Management depends on the severity and may involve conservative treatment or surgical intervention. Prevention is crucial in reducing the incidence of abdominal trauma in children.
TEST BANK For Community Health Nursing A Canadian Perspective, 5th Edition by...Donc Test
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Histololgy of Female Reproductive System.pptxAyeshaZaid1
Dive into an in-depth exploration of the histological structure of female reproductive system with this comprehensive lecture. Presented by Dr. Ayesha Irfan, Assistant Professor of Anatomy, this presentation covers the Gross anatomy and functional histology of the female reproductive organs. Ideal for students, educators, and anyone interested in medical science, this lecture provides clear explanations, detailed diagrams, and valuable insights into female reproductive system. Enhance your knowledge and understanding of this essential aspect of human biology.
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.
Osteoporosis - Definition , Evaluation and Management .pdfJim Jacob Roy
Osteoporosis is an increasing cause of morbidity among the elderly.
In this document , a brief outline of osteoporosis is given , including the risk factors of osteoporosis fractures , the indications for testing bone mineral density and the management of osteoporosis
These lecture slides, by Dr Sidra Arshad, offer a quick overview of the physiological basis of a normal electrocardiogram.
Learning objectives:
1. Define an electrocardiogram (ECG) and electrocardiography
2. Describe how dipoles generated by the heart produce the waveforms of the ECG
3. Describe the components of a normal electrocardiogram of a typical bipolar lead (limb II)
4. Differentiate between intervals and segments
5. Enlist some common indications for obtaining an ECG
6. Describe the flow of current around the heart during the cardiac cycle
7. Discuss the placement and polarity of the leads of electrocardiograph
8. Describe the normal electrocardiograms recorded from the limb leads and explain the physiological basis of the different records that are obtained
9. Define mean electrical vector (axis) of the heart and give the normal range
10. Define the mean QRS vector
11. Describe the axes of leads (hexagonal reference system)
12. Comprehend the vectorial analysis of the normal ECG
13. Determine the mean electrical axis of the ventricular QRS and appreciate the mean axis deviation
14. Explain the concepts of current of injury, J point, and their significance
Study Resources:
1. Chapter 11, Guyton and Hall Textbook of Medical Physiology, 14th edition
2. Chapter 9, Human Physiology - From Cells to Systems, Lauralee Sherwood, 9th edition
3. Chapter 29, Ganong’s Review of Medical Physiology, 26th edition
4. Electrocardiogram, StatPearls - https://www.ncbi.nlm.nih.gov/books/NBK549803/
5. ECG in Medical Practice by ABM Abdullah, 4th edition
6. Chapter 3, Cardiology Explained, https://www.ncbi.nlm.nih.gov/books/NBK2214/
7. ECG Basics, http://www.nataliescasebook.com/tag/e-c-g-basics
Basavarajeeyam is a Sreshta Sangraha grantha (Compiled book ), written by Neelkanta kotturu Basavaraja Virachita. It contains 25 Prakaranas, First 24 Chapters related to Rogas& 25th to Rasadravyas.
Here is the updated list of Top Best Ayurvedic medicine for Gas and Indigestion and those are Gas-O-Go Syp for Dyspepsia | Lavizyme Syrup for Acidity | Yumzyme Hepatoprotective Capsules etc
1. Amino Acids
Amino Acids are the building units of proteins. Proteins are
polymers of amino acids linked together by what is called
“ Peptide bond”.
There are about 300 amino acids occur in nature. Only 20 of
them occur in proteins.
Structure of amino acids:
Each amino acid has 4 different groups attached to α- carbon
( which is C-atom next to COOH). These 4 groups are : amino
group, COOH gp,
Hydrogen atom and side
Chain (R)
R
2. • At physiological pH (7.4), -COOH gp is dissociated forming a
negatively charged carboxylate ion (COO-) and amino gp is
protonated forming positively charged ion (NH3
+) forming
Zwitter ion
• N.B. Proline is an imino acid not amino acid
CLASSIFICATION OF AMINO ACIDS
I- Chemical classification: According to number of COOH and
NH2 groups i.e. according to net charge on amino acid.
A- Monobasic, monocarboxylic amino acids i.e. neutral or
uncharged:
R
3. Subclassification of neutral amino acids:
All structures are required
1- Glycine R= H
2- Alanine R= CH3
3- Branched chain amino acids: R is branched such as in:
a - Valine R= isopropyl gp
b- Leucine R= isobutyl gp
c- Isoleucine R = is isobutyl
R is isobutyl in both leucine and isoleucine but branching is
different: in leucine → branching occurs on γ carbon
in isoleucine→ branching occurs on β- carbon
4- Neutral Sulfur containing amino acids:
e.g. Cysteine and Methionine.
5- Neutral, hydroxy amino acids:
e.g. Serine and Threonine
4. 6- Neutral aromatic amino acids:
a- Phenyl alanine : It’s alanine in which one hydrogen of CH3 is
substituted with phenyl group. So it’s called
phenyl alanine
b- Tyrosine: - it is P- hydroxy phenyl alanine
- it is classified as phenolic amino acid
c- Tryptophan: as it contains indole ring so it is classified as
heterocyclic amino acid
7- Neutral heterocyclic amino acids:
a- Tryptophan: contains indole ring
b- Proline: In proline, amino group enters in the ring formation
being α-imino gp so proline is an α-imino acid
rather than α-amino acid
5. B- Basic amino acids: Contain two or more NH2 groups or
nitrogen atoms that act as base i.e. can
bind proton.
At physiological pH, basic amino acids will be positively charged.
e.g.
a- Lysine
b- Arginine: contains guanido group
c- Histidine: is an example on basic heterocyclic amino acids
6. C- Acidic Amino acids: at physiological pH will carry negative
charge.
e.g. Aspartic acid (aspartate) and Glutamic acid (glutamate).
Aspargine and Glutamine: They are amide forms of aspartate and
glutamate in which side chain COOH groups are amidated.
They are classified as neutral amino acids.
7. II- Classification according to polarity of side chain (R):
A- Polar amino acids: in which R contains polar hydrophilic group so
can forms hydrogen bond with H2O. In those amino acids, R may
contain:
1- OH group : as in serine, threonine and tyrosine
2- SH group : as in cysteine
3- Amide group: as in glutamine and aspargine
4- NH2 group or nitrogen act as a base (basic amino acids ): as lysine,
arginine and histidine
5- COOH group ( acidic amino acids): as aspartic and glutamic .
B- Non polar amino acids:
R is alkyl hydrophobic group which can’t enter in hydrogen bond
formation. 9 amino acids are non polar ( glycine, alanine, valine, leucine,
isoleucine, phenyl alanine, tryptophan, proline and methionine)
8.
9. III- Nutritional classification:
1- Essential amino acids: These amino acids can’t be formed in the
body and so, it is essential to be taken in diet. Their deficiency
affects growth, health and protein synthesis.
2- Semi-essential amino acids: These are formed in the body but not
in sufficient amount for body requirements especially in children.
Summary of essential and semiessential amino acids:
(Villa HM = Ten Thousands Pound)
V= valine i= isoleucine l= lysine l= leucine
A = arginine* H= histidine* M= methionine
T= tryptophan Th= threonine P= phenyl alanine
*= arginine and histidine are semi-essential
3- Non-essential amino acids: These are the rest of amino acids that
are formed in the body in amount enough for adults and children.
They are the remaining 10 amino acids.
10. IV- Metabolic classification: according to metabolic or degradation
products of amino acids they may be:
1- Ketogenic amino acids: which give ketone bodies . Lysine and
Leucine are the only pure ketogenic amino acids.
2- Mixed ketogenic and glucogenic amino acids: which give both
ketonbodies and glucose.These are: isoleucine, phenyl alanine, tyrosine
and tryptophan.
3- Glucogenic amino acids: Which give glucose. They include the rest
of amino acids. These amino acids by catabolism yields products that
enter in glycogen and glucose formation.
11. Amphoteric properties of amino acids: that is they have both basic and
acidic groups and so can act as base or acid.
Neutral amino acids (monobasic, monocarboxylic) exist in aqueous solution as “
Zwitter ion” i.e. contain both positive and negative charge. Zwitter ion is electrically
neutral and can’t migrate into electric field.
Isoelectric point (IEP) = is the pH at which the zwitter ion is formed. e.g IEP
of alanine is 6
Chemical properties of amino acids:
1- Reactions due to COOH group:
-Salt formation with alkalis, ester formation with alcohols, amide formation with
amines and decarboxylation
-2- Reactions due toNH2 group: deamination and reaction with ninhydrin
reagent.
-Ninhydrin reagent reacts with amino group of amino acid yielding blue colored
product. The intensity of blue color indicates quantity of amino acids present.
(A zwitterion formerly called a dipolar ion, is a molecule with two or
more functional groups, of which at least one has a positive and one has a
negative electrical charge and the net charge of the entire molecule is zero. Because
they contain at least one positive and one negative charge, zwitterions are also
sometimes called inner salts)
12. Ninhydrine can react with imino acids as proline and hydroxy
proline but gives yellow color.
3- Reactions due to side chain (R):
1- Millon reaction: for tyrosine gives red colored mass
2- Rosenheim reaction: for trptophan and gives violet ring.
3- Pauly reaction: for imidazole ring of histidine: gives yellow to
reddish product
4- Sakagushi test: for guanido group of arginine andgives red
color.
5- Lead sulfide test (sulfur test): for sulfur containing amino acids
as cysteine give brown color.
13. Peptides and Proteins
20 amino acids are commonly found in protein.
These 20 amino acids are linked together through “peptide bond
forming peptides and proteins.
- The chains containing less than 50 amino acids are called
“peptides”, while those containing greater than 50 amino acids are
called “proteins”.
Peptide bond formation:
α-carboxyl group of one amino acid (with side chain R1)
forms a covalent peptide bond with α-amino group of another
amino acid ( with the side chain R2) by removal of a molecule of
water. The result is : Dipeptide ( i.e. Two amino acids linked by one
peptide bond). By the same way, the dipeptide can then forms a
second peptide bond with a third amino acid (with side chain R3) to
give Tripeptide. Repetition of this process generates a polypeptide
or protein of specific amino acid sequence.
14. Peptide bond formation:
- Each polypeptide chain starts on the left side by free amino group of
the first amino acid enter in chain formation . It is termed (N- terminus).
- Each polypeptide chain ends on the right side by free COOH group of
the last amino acid and termed (C-terminus).
15. Examples on Peptides:
1- Dipeptide ( tow amino acids joined by one peptide bond):
Example: Aspartame which acts as sweetening agent being used in
replacement of cane sugar. It is composed of aspartic acid and
phenyl alanine.
2- Tripeptides ( 3 amino acids linked by two peptide bonds).
Example: GSH which is formed from 3 amino acids: glutamic acid,
cysteine and glycine. It helps in absorption of amino acids, protects
against hemolysis of RBC by breaking H2O2 which causes cell
damage.
3- Octapeptides: (8 amino acids)
Examples: Two hormones; oxytocine and vasopressin (ADH).
4- Polypeptides: 10- 50 amino acids: e.g. Insulin hormone
16. Protein structure:
There are four levels of protein structure (primary,
secondary, tertiary and quaternary)
Primary structure:
• The primary structure of a protein is its
unique sequence of amino acids.
– Lysozyme, an enzyme that attacks bacteria,
consists of a polypeptide chain of 129
amino acids.
– The precise primary structure of a protein is
determined by inherited genetic
information.
– At one end is an amino acid with a free
amino group the (the N-terminus) and at the
other is an amino acid with a free carboxyl
group the (the C-terminus).
17. High orders of Protein structure
• A functional protein is not just a polypeptide chain, but one or
more polypeptides precisely twisted, folded and coiled into a
molecule of unique shape (conformation). This conformation is
essential for some protein function e.g. Enables a protein to
recognize and bind specifically to another molecule e.g.
hormone/receptor; enzyme/substrate and antibody/antigen.
•
18. 2- Secondary structure:
Results from hydrogen bond
formation between hydrogen of –NH
group of peptide bond and the carbonyl
oxygen of another peptide bond.
According to H-bonding there are two
main forms of secondary structure:
α-helix: It is a spiral structure
resulting from hydrogen bonding
between one peptide bond and the fourth
one
β-sheets: is another form of secondary
structure in which two or more
polypeptides (or segments of the same
peptide chain) are linked together by
hydrogen bond between H- of NH- of one
chain and carbonyl oxygen of adjacent
chain (or segment).
19. Hydrogen bonding in α-helix: In the α-helix CO of the one amino
acid residue forms H-bond with NH of the forth one.
Supersecondary structure or Motifs :
occurs by combining secondary structure.
The combination may be: α-helix- turn- α-helix- turn…..etc
Or: β-sheet -turn- β-sheet-turn………etc
Or: α-helix- turn- β-sheet-turn- α-helix
Turn (or bend): is short segment of polypeptides (3-4 amino acids)
that connects successive secondary structures.
e.g. β-turn: is small polypeptide that connects successive strands of β-
sheets.
20. • Tertiary structure is
determined by a variety of
interactions (bond formation)
among R groups and between R
groups and the polypeptide
backbone.
a. The weak interactions include:
Hydrogen bonds among polar
side chains
Ionic bonds between
charged R groups ( basic and
acidic amino acids)
Hydrophobic
interactions among
hydrophobic ( non polar) R
groups.
21. b. Strong covalent bonds include disulfide bridges, that form
between the sulfhydryl groups (SH) of cysteine monomers,
stabilize the structure.
Insulin, chemical structure and metabolism. Insulinis a
polypeptide hormone formed, after elimination of C peptide
by hydrolysis, of two chains of 21 and 30 amino acids,
connected by two disulfide bridges. It is secreted by the ß
cells of the islets of Langerhans of the pancreas and exerts
an hypoglycemic action.
22. • Quaternary structure: results from the aggregation (combination) of two
or more polypeptide subunits held together by non-covalent interaction like H-
bonds, ionic or hydrophobic interactions.
• Examples on protein having quaternary structure:
– Collagen is a fibrous protein of three polypeptides (trimeric) that are
supercoiled like a rope.
• This provides the structural strength for their role in connective tissue.
– Hemoglobin is a globular protein with four polypeptide chains (tetrameric)
– Insulin : two polypeptide chains (dimeric)
23.
24. Classification of proteins
I- Simple proteins:
i.e. on hydrolysis gives only amino acids
Examples:
1- Albumin and globulins: present in egg, milk and blood
They are proteins of high biological value i.e. contain all essential
amino acids and easily digested.
Types of globulins:
α1 globulin: e.g. antitrypsin: see later
α2 globulin: e.g. hepatoglobin: protein that binds hemoglobin to
prevent its excretion by the kidney
β-globulin: e.g. transferrin: protein that transport iron
γ-globulins = Immunoglobulins (antibodies) : responsible for
immunity.
25. 2- Globins (Histones): They are basic proteins rich in histidine amino
acid.
They are present in : a - combined with DNA
b - combined with heme to form hemoglobin of
RBCs.
3- Gliadines are the proteins present in cereals.
4- Scleroproteins: They are structural proteins, not digested.
include: keratin, collagen and elastin.
a- α-keratin: protein found in hair, nails, enamel of teeth and outer layer
of skin.
• It is α-helical polypeptide chain, rich in cysteine and hydrophobic
(non polar) amino acids so it is water insoluble.
b- collagens: protein of connective tissues found in bone, teeth,
cartilage, tendons, skin and blood vessels.
26. • Collagen may be present as gel e.g. in extracellular matrix
or in vitreous humor of the eye.
• Collagens are the most important protein in mammals.
They form about 30% of total body proteins.
• There are more than 20 types of collagens, the most
common type is collagen I which constitutes about 90% of
cell collagens.
• Structure of collagen: three helical polypeptide chains
(trimeric) twisted around each other forming triplet-helix
molecule.
• ⅓ of structure is glycine, 10% proline, 10% hydroxyproline
and 1% hydroxylysine. Glycine is found in every third
position of the chain. The repeating sequence –Gly-X-Y-,
where X is frequently proline and Y is often hydroxyproline
and can be hydroxylysine.
27. Solubility: collagen is insoluble in all solvents and not digested.
• When collagen is heated with water or dil. HCl it will be converted
into gelatin which is soluble , digestible and used as diet ( as jelly).
Gelatin is classified as derived protein.
Some collagen diseases:
1- Scurvy: disease due to deficiency of vitamin C which is important
coenzyme for conversion of proline into hydroxyproline and lysine into
hydroxylysine. Thus, synthesis of collagen is decreased leading to
abnormal bone development, bleeding, loosing of teeth and swollen
gum.
2- Osteogenesis Imperfecta (OI): Inherited disease resulting from
genetic deficiency or mutation in gene that synthesizes collagen type I
leading to abnormal bone formation in babies and frequent bone
fracture in children. It may be lethal.
28. C- Elastin: present in walls of large blood vessels (such as aorta). It is
very important in lungs, elastic ligaments, skin, cartilage, ..
It is elastic fiber that can be stretched to several times as its normal
length.
Structure: composed of 4 polypeptide chains (tetramer), similar to
collagen being having 33% glycine and rich in proline but
in that it has low hydroxyproline and absence of hydroxy
lysine.
Emphysema: is a chronic obstructive lung disease (obstruction of air
ways) resulting from deficiency of α1-antitrypsin
particularly in cigarette smokers.
Role of α1-antitrypsin: Elastin is a lung protein. Smoke stimulate
enzyme called elastase to be secreted form
neutrophils (in lung). Elastase cause
destruction of elastin of lung.
29. α1-antitrypsin is an enzyme (secreted from liver) and inhibit elastase and
prevent destruction of elastin. So deficiency of α1-antitrypsin especially
in smokers leads to degradation of lung and destruction of lung ( loss of
elasticity of lung, a disease called emphysema.
Conjugated proteins
i.e. On hydrolysis, give protein part and non protein part and
subclassified into:
1- Phosphoproteins: These are proteins conjugated with phosphate
group. Phosphorus is attached to oh group of serine or threonine.
e.g. Casein of milk and vitellin of yolk.
30. 2- Lipoproteins:
These are proteins conjugated with lipids.
Functions: a- help lipids to transport in blood
b- Enter in cell membrane structure helping lipid soluble
substances to pass through cell membranes.
3- Glycoproteins:
proteins conjugated with sugar (carbohydrate)
e.g. – Mucin
- Some hormones such as erythropoeitin
- present in cell membrane structure
- blood groups.
4- Nucleoproteins: These are basic proteins ( e.g. histones)
conjugated with nucleic acid (DNA or RNA).
e.g. a- chromosomes: are proteins conjugated with DNA
b- Ribosomes: are proteins conjugated with RNA
31. 5- Metalloproteins: These are proteins conjugated with metal like
iron, copper, zinc, ……
a- Iron-containing proteins: Iron may present in heme such as in
- hemoglobin (Hb)
- myoglobin ( protein of skeletal muscles and cardiacmuscle),
- cytochromes,
- catalase, peroxidases (destroy H2O2)
- tryptophan pyrrolase (desrtroy indole ring of tryptophan).
Iron may be present in free state ( not in heme) as in:
- Ferritin: Main store of iron in the body. ferritin is present in liver,
spleen and bone marrow.
- Hemosidrin: another iron store.
- Transferrin: is the iron carrier protein in plasma.
32. b- Copper containing proteins:
e.g. - Ceruloplasmin which oxidizes ferrous ions into ferric ions.
- Oxidase enzymes such as cytochrome oxidase.
c- Zn containing proteins: e.g. Insulin and carbonic anhydrase
d- Mg containing proteins:e.g. Kinases and phosphatases.
6-Chromoproteins: These are proteins conjugated with pigment. e.g.
- All proteins containing heme (Hb, myoglobin, ………..)
- Melanoprotein*:e.g proteins of hair or iris which contain melanin.
Derived proteins
Produced from hydrolysis of simple proteins.
e.g. - Gelatin: from hydrolysis of collagen
- Peptone: from hydrolysis of albumin
*A hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein,
is a protein thatcontains a heme prosthetic group. They are a large class of
metalloproteins. The heme group confers functionality, which can include oxygen
carrying oxygen reduction, electron transfer, and other processes.