The document discusses the basic structures and properties of amino acids and proteins. It provides details on the 20 standard amino acids, including their abbreviations and the characteristics of their R-groups. The amino acids are classified as neutral, acidic, basic, or polar based on the properties of their side chains. Essential amino acids cannot be synthesized by the human body and must be obtained through diet.
Biochemistry is the study of biological processes at the cellular and molecular level by applying principles of chemistry. It emerged in the early 20th century through combining chemistry, biology, and physiology to study living systems. Biochemistry examines the structure and behavior of complex molecules in biological material and how they interact to form cells, tissues, and whole organisms. It also studies the thousands of chemical reactions that occur in cells, how they are precisely regulated to maintain life, and the molecules like carbohydrates, proteins, lipids, and nucleic acids that are common to all organisms.
- Amino acids exist in two forms, L and D, depending on their stereoisomer configuration. Only L-amino acids are used in protein synthesis.
- Amino acids are amphoteric, meaning they can act as acids or bases depending on the pH. At low pH they are protonated and at high pH they are deprotonated.
- In solution, amino acids exist as zwitterions - molecules with both positive and negative charges that cancel out to have no overall charge. The isoelectric point is the pH at which the zwitterion form dominates.
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.
Detailed Amino acid structure, Zwitter ions, acid base properties of Amino acids, Chirality, L and D forms of amino acids,standard and non standard amino acids, Essential and non essential amino acids,Learn all amino acids, their properties in detail,methods to quantify amino acids
1) ATP is the energy currency of cells and is composed of adenine, ribose, and three phosphate groups.
2) ATP is regenerated as cells use it to power cellular work through a process where its terminal phosphate bond is broken through hydrolysis, releasing energy.
3) The energy from exergonic reactions like cellular respiration is used to regenerate ATP by adding a phosphate back to ADP, driven by ATP synthase in the mitochondria.
The document summarizes electron transport and oxidative phosphorylation. It describes how electrons from NADH and FADH2 are transported via carriers in the mitochondrial electron transport system to oxygen, with energy released used to synthesize ATP. Protons are pumped from the mitochondrial matrix to the intermembrane space, building a proton gradient that drives ATP synthesis by ATP synthase as protons flow back into the matrix. This chemiosmotic coupling allows efficient conversion of electron potential energy to chemical energy in the form of ATP.
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.
I have prepare this slide thinking that it will help students .I have collected different photos and videos from internet please comment and if you need any slides for a topics . i will prepare the slide .
Biochemistry is the study of biological processes at the cellular and molecular level by applying principles of chemistry. It emerged in the early 20th century through combining chemistry, biology, and physiology to study living systems. Biochemistry examines the structure and behavior of complex molecules in biological material and how they interact to form cells, tissues, and whole organisms. It also studies the thousands of chemical reactions that occur in cells, how they are precisely regulated to maintain life, and the molecules like carbohydrates, proteins, lipids, and nucleic acids that are common to all organisms.
- Amino acids exist in two forms, L and D, depending on their stereoisomer configuration. Only L-amino acids are used in protein synthesis.
- Amino acids are amphoteric, meaning they can act as acids or bases depending on the pH. At low pH they are protonated and at high pH they are deprotonated.
- In solution, amino acids exist as zwitterions - molecules with both positive and negative charges that cancel out to have no overall charge. The isoelectric point is the pH at which the zwitterion form dominates.
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.
Detailed Amino acid structure, Zwitter ions, acid base properties of Amino acids, Chirality, L and D forms of amino acids,standard and non standard amino acids, Essential and non essential amino acids,Learn all amino acids, their properties in detail,methods to quantify amino acids
1) ATP is the energy currency of cells and is composed of adenine, ribose, and three phosphate groups.
2) ATP is regenerated as cells use it to power cellular work through a process where its terminal phosphate bond is broken through hydrolysis, releasing energy.
3) The energy from exergonic reactions like cellular respiration is used to regenerate ATP by adding a phosphate back to ADP, driven by ATP synthase in the mitochondria.
The document summarizes electron transport and oxidative phosphorylation. It describes how electrons from NADH and FADH2 are transported via carriers in the mitochondrial electron transport system to oxygen, with energy released used to synthesize ATP. Protons are pumped from the mitochondrial matrix to the intermembrane space, building a proton gradient that drives ATP synthesis by ATP synthase as protons flow back into the matrix. This chemiosmotic coupling allows efficient conversion of electron potential energy to chemical energy in the form of ATP.
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.
I have prepare this slide thinking that it will help students .I have collected different photos and videos from internet please comment and if you need any slides for a topics . i will prepare the slide .
This document summarizes key chemistry concepts related to the building blocks of life. It covers the elements, atoms, and molecules that make up living organisms. It also describes the four main types of organic compounds - carbohydrates, lipids, proteins, and nucleic acids - and provides examples of each. Water is highlighted for its importance as a solvent and in biological processes and reactions.
Lipids are a heterogeneous group of compounds including fats, oils, steroids, waxes and related compounds. They are insoluble in water but soluble in nonpolar solvents. Lipids serve many important functions such as energy storage, structural components of cell membranes, and transport of fat-soluble vitamins. Abnormal lipid chemistry or metabolism can lead to diseases like obesity, atherosclerosis and diabetes. Lipids are classified into simple lipids like fats and oils, complex lipids containing additional groups like phospholipids and glycolipids, and derived lipids including fatty acids, glycerol and steroids.
Carbohydrates provide the body with heat and can be classified into simple or complex forms. They consist of carbon, hydrogen, and oxygen and include sugars, starches, and fibers. Carbohydrates are grouped into monosaccharides, disaccharides, trisaccharides, polysaccharides, and heterosaccharides. They can also be categorized as simple starchy, complex starchy, or complex fibrous carbohydrates. Simple carbohydrates like glucose and sucrose are made of 1-2 sugar molecules while complex starches like whole grains have longer sugar chains. Complex fibrous carbohydrates are found in green vegetables and provide vitamins, minerals and fiber.
This document provides an introduction to biochemistry, including definitions and key concepts. It discusses biochemistry as the study of the structure and function of biomolecules in living organisms. The document outlines that living things are composed of common elements like carbon, hydrogen, oxygen, nitrogen and complex macromolecules including carbohydrates, proteins, nucleic acids and lipids. It also describes important cellular structures like the cell membrane, nucleus, mitochondria and chloroplasts. Finally, the document provides overviews of the four major macromolecule classes and how pH and buffers are important concepts in biochemistry.
Anomers are carbohydrate structures that differ only in the configuration of the hydroxyl group on the anomeric carbon. The anomeric carbon is the carbon atom involved in the cyclic formation of carbohydrates. Examples of anomers are alpha-glucose and beta-glucose which have different hydroxyl group positions on the first carbon. Epimers differ at only one other chiral carbon, not the anomeric carbon, while mutarotation is the process where glucose anomers interconvert between ring forms in solution.
Nucleic acids are organic biomolecules that contain heterocyclic rings. They are composed of nucleotides which contain a nitrogenous base, pentose sugar, and phosphate group. Nucleotides polymerize to form long chains with phosphodiester bonds between the sugar and phosphate groups. There are four nucleotides in DNA: adenine, cytosine, guanine, and thymine. Nucleic acids function to store and transfer genetic information, with DNA controlling cellular functions and RNA involved in protein synthesis.
Disaccharides are double sugars that yield two simple sugars called monosaccharides upon hydrolysis. The three main disaccharides are sucrose, maltose, and lactose. They differ in their solubility, with sucrose being very soluble, maltose fairly soluble, and lactose only slightly soluble. Disaccharides are formed through a dehydration synthesis reaction combining two monosaccharides. Their structures depend on the type of glycosidic linkage between the monosaccharides. This determines their properties such as whether they are reducing sugars or able to undergo fermentation.
This presentation is made for F.Y.Bsc. Students.
The presentation includes the General Properties of Carbohydrate and the classification of carbohydrates.
This document provides information about lipids and fatty acids. It begins with an outline of chapter topics on the chemistry and classification of lipids. It then defines lipids and lists their main functions in the body. Lipids are classified as simple, complex, or derived, and as saponifiable or non-saponifiable. Key reactions for lipids include hydrolysis. Fatty acids are classified based on saturation and chain length. Essential fatty acids, which must be obtained through diet, are discussed. Neutral fats are described as triacylglycerols composed of glycerol and fatty acids.
This document discusses protein structure and function. It begins by defining proteins and their essential roles in the human body. It then describes the general characteristics of proteins, such as their chemical composition and functions. The document classifies proteins based on their composition, axial ratio, and biological functions. It explains the different levels of protein structure from primary to quaternary, focusing on secondary structure elements like alpha helices and beta sheets. The roles of hydrogen bonding, disulfide bridges, and ionic bonds in tertiary and quaternary structure are also described.
Biochemistry is the study of biological processes at the cellular and molecular level through the application of chemistry. It emerged in the early 20th century as scientists combined chemistry, biology, and physiology to study the complex molecules found in living systems and how they interact to form cells, tissues, and whole organisms. Biochemistry examines the chemical reactions that take place in living things and how cells use energy to maintain their highly organized state despite containing thousands of regulated chemical reactions.
Peptide bonds form during translation within ribosomes and connect amino acids into polypeptide chains that fold into protein structures. A peptide bond is a covalent bond formed through a dehydration synthesis reaction between the carboxyl group of one amino acid and the amine group of the next. This reaction involves the loss of a water molecule as the carboxyl oxygen and amine hydrogen are removed to connect the amino acids. Peptide bonds make up the backbone of proteins by linking the 20 common amino acids together end to end.
This ppt explains the structure of carbohydrates and its occurrence. It explains the linear chain structure, haworth projection, fischer projection and hemiacetal structure of carbohydrates.
Enzymes catalyze chemical reactions in cells without being altered. Glycolysis uses enzymes like dehydrogenase to break down glucose into pyruvate, producing ATP in the cytoplasm. The citric acid cycle uses enzymatic reactions in mitochondria to further oxidize pyruvate, producing more ATP. Oxidative phosphorylation is the final step of respiration, using an electron transport chain and ATP synthase to generate most of the cell's ATP through phosphorylation.
Biological oxidation involves the transfer of electrons, with oxidation being the removal of electrons and reduction being the gain of electrons. Higher life forms rely completely on oxygen for life processes like respiration, where cells derive energy from the reaction of hydrogen and oxygen to produce water. However, many reactions in living systems occur without oxygen involvement, catalyzed by dehydrogenases. Oxygen is also required to treat respiratory and cardiac failure. Redox reactions can be expressed as half reactions with a reducing agent donating electrons and an oxidizing agent accepting electrons. The redox potential measures a substance's affinity for electrons. Enzymes involved in redox reactions include oxidases, dehydrogenases, hydroperoxidases, and oxygenases.
The document discusses biochemistry for medics and provides information on amino acids. It defines that amino acids are the monomer units that make up protein polypeptides and participate in various cellular functions. It classifies amino acids based on structure, side chains, nutritional requirements, and metabolic fate. The document also discusses the structures, properties, reactions and significance of different amino acids. Testing methods to identify specific amino acids are also outlined.
Biochemistry of water - presentation given by Dr. Karthikeyan Pethusamy at department of biochemistry, Maulana Azad Medical College. To make slides simple, less information is given in slides. More information was shared during the presentation.
1. The document provides an introduction to biochemistry including defining it as the science concerned with chemical basis of life and chemical constituents of living cells.
2. It describes the key components of living matter including water, inorganic substances, and organic biomolecules.
3. The key cellular organelles such as nucleus, mitochondria, endoplasmic reticulum, Golgi complex, lysosomes, and their functions are outlined.
This document summarizes standard amino acids. It discusses how amino acids are the building blocks of proteins and join together in chains. It then describes the history of amino acid discoveries starting in the early 19th century. The rest of the document details the 20 standard amino acids that make up proteins, including their structures, properties, and remarks about each amino acid.
Protein structureandfunction 2018_fall3 (1)SaiBadugu
This document provides an overview of protein structure and function. It begins by outlining the learning objectives, which include explaining the primary, secondary, tertiary, and quaternary structure of proteins as well as specific examples of protein function. The document then covers the individual amino acids that make up proteins, categorizing them based on properties like charge, size, hydrophobicity, and whether they contain aromatic, hydroxyl, sulfur, or acidic/basic functional groups. It discusses how these various amino acid properties and interactions determine protein structure and function.
This document summarizes key chemistry concepts related to the building blocks of life. It covers the elements, atoms, and molecules that make up living organisms. It also describes the four main types of organic compounds - carbohydrates, lipids, proteins, and nucleic acids - and provides examples of each. Water is highlighted for its importance as a solvent and in biological processes and reactions.
Lipids are a heterogeneous group of compounds including fats, oils, steroids, waxes and related compounds. They are insoluble in water but soluble in nonpolar solvents. Lipids serve many important functions such as energy storage, structural components of cell membranes, and transport of fat-soluble vitamins. Abnormal lipid chemistry or metabolism can lead to diseases like obesity, atherosclerosis and diabetes. Lipids are classified into simple lipids like fats and oils, complex lipids containing additional groups like phospholipids and glycolipids, and derived lipids including fatty acids, glycerol and steroids.
Carbohydrates provide the body with heat and can be classified into simple or complex forms. They consist of carbon, hydrogen, and oxygen and include sugars, starches, and fibers. Carbohydrates are grouped into monosaccharides, disaccharides, trisaccharides, polysaccharides, and heterosaccharides. They can also be categorized as simple starchy, complex starchy, or complex fibrous carbohydrates. Simple carbohydrates like glucose and sucrose are made of 1-2 sugar molecules while complex starches like whole grains have longer sugar chains. Complex fibrous carbohydrates are found in green vegetables and provide vitamins, minerals and fiber.
This document provides an introduction to biochemistry, including definitions and key concepts. It discusses biochemistry as the study of the structure and function of biomolecules in living organisms. The document outlines that living things are composed of common elements like carbon, hydrogen, oxygen, nitrogen and complex macromolecules including carbohydrates, proteins, nucleic acids and lipids. It also describes important cellular structures like the cell membrane, nucleus, mitochondria and chloroplasts. Finally, the document provides overviews of the four major macromolecule classes and how pH and buffers are important concepts in biochemistry.
Anomers are carbohydrate structures that differ only in the configuration of the hydroxyl group on the anomeric carbon. The anomeric carbon is the carbon atom involved in the cyclic formation of carbohydrates. Examples of anomers are alpha-glucose and beta-glucose which have different hydroxyl group positions on the first carbon. Epimers differ at only one other chiral carbon, not the anomeric carbon, while mutarotation is the process where glucose anomers interconvert between ring forms in solution.
Nucleic acids are organic biomolecules that contain heterocyclic rings. They are composed of nucleotides which contain a nitrogenous base, pentose sugar, and phosphate group. Nucleotides polymerize to form long chains with phosphodiester bonds between the sugar and phosphate groups. There are four nucleotides in DNA: adenine, cytosine, guanine, and thymine. Nucleic acids function to store and transfer genetic information, with DNA controlling cellular functions and RNA involved in protein synthesis.
Disaccharides are double sugars that yield two simple sugars called monosaccharides upon hydrolysis. The three main disaccharides are sucrose, maltose, and lactose. They differ in their solubility, with sucrose being very soluble, maltose fairly soluble, and lactose only slightly soluble. Disaccharides are formed through a dehydration synthesis reaction combining two monosaccharides. Their structures depend on the type of glycosidic linkage between the monosaccharides. This determines their properties such as whether they are reducing sugars or able to undergo fermentation.
This presentation is made for F.Y.Bsc. Students.
The presentation includes the General Properties of Carbohydrate and the classification of carbohydrates.
This document provides information about lipids and fatty acids. It begins with an outline of chapter topics on the chemistry and classification of lipids. It then defines lipids and lists their main functions in the body. Lipids are classified as simple, complex, or derived, and as saponifiable or non-saponifiable. Key reactions for lipids include hydrolysis. Fatty acids are classified based on saturation and chain length. Essential fatty acids, which must be obtained through diet, are discussed. Neutral fats are described as triacylglycerols composed of glycerol and fatty acids.
This document discusses protein structure and function. It begins by defining proteins and their essential roles in the human body. It then describes the general characteristics of proteins, such as their chemical composition and functions. The document classifies proteins based on their composition, axial ratio, and biological functions. It explains the different levels of protein structure from primary to quaternary, focusing on secondary structure elements like alpha helices and beta sheets. The roles of hydrogen bonding, disulfide bridges, and ionic bonds in tertiary and quaternary structure are also described.
Biochemistry is the study of biological processes at the cellular and molecular level through the application of chemistry. It emerged in the early 20th century as scientists combined chemistry, biology, and physiology to study the complex molecules found in living systems and how they interact to form cells, tissues, and whole organisms. Biochemistry examines the chemical reactions that take place in living things and how cells use energy to maintain their highly organized state despite containing thousands of regulated chemical reactions.
Peptide bonds form during translation within ribosomes and connect amino acids into polypeptide chains that fold into protein structures. A peptide bond is a covalent bond formed through a dehydration synthesis reaction between the carboxyl group of one amino acid and the amine group of the next. This reaction involves the loss of a water molecule as the carboxyl oxygen and amine hydrogen are removed to connect the amino acids. Peptide bonds make up the backbone of proteins by linking the 20 common amino acids together end to end.
This ppt explains the structure of carbohydrates and its occurrence. It explains the linear chain structure, haworth projection, fischer projection and hemiacetal structure of carbohydrates.
Enzymes catalyze chemical reactions in cells without being altered. Glycolysis uses enzymes like dehydrogenase to break down glucose into pyruvate, producing ATP in the cytoplasm. The citric acid cycle uses enzymatic reactions in mitochondria to further oxidize pyruvate, producing more ATP. Oxidative phosphorylation is the final step of respiration, using an electron transport chain and ATP synthase to generate most of the cell's ATP through phosphorylation.
Biological oxidation involves the transfer of electrons, with oxidation being the removal of electrons and reduction being the gain of electrons. Higher life forms rely completely on oxygen for life processes like respiration, where cells derive energy from the reaction of hydrogen and oxygen to produce water. However, many reactions in living systems occur without oxygen involvement, catalyzed by dehydrogenases. Oxygen is also required to treat respiratory and cardiac failure. Redox reactions can be expressed as half reactions with a reducing agent donating electrons and an oxidizing agent accepting electrons. The redox potential measures a substance's affinity for electrons. Enzymes involved in redox reactions include oxidases, dehydrogenases, hydroperoxidases, and oxygenases.
The document discusses biochemistry for medics and provides information on amino acids. It defines that amino acids are the monomer units that make up protein polypeptides and participate in various cellular functions. It classifies amino acids based on structure, side chains, nutritional requirements, and metabolic fate. The document also discusses the structures, properties, reactions and significance of different amino acids. Testing methods to identify specific amino acids are also outlined.
Biochemistry of water - presentation given by Dr. Karthikeyan Pethusamy at department of biochemistry, Maulana Azad Medical College. To make slides simple, less information is given in slides. More information was shared during the presentation.
1. The document provides an introduction to biochemistry including defining it as the science concerned with chemical basis of life and chemical constituents of living cells.
2. It describes the key components of living matter including water, inorganic substances, and organic biomolecules.
3. The key cellular organelles such as nucleus, mitochondria, endoplasmic reticulum, Golgi complex, lysosomes, and their functions are outlined.
This document summarizes standard amino acids. It discusses how amino acids are the building blocks of proteins and join together in chains. It then describes the history of amino acid discoveries starting in the early 19th century. The rest of the document details the 20 standard amino acids that make up proteins, including their structures, properties, and remarks about each amino acid.
Protein structureandfunction 2018_fall3 (1)SaiBadugu
This document provides an overview of protein structure and function. It begins by outlining the learning objectives, which include explaining the primary, secondary, tertiary, and quaternary structure of proteins as well as specific examples of protein function. The document then covers the individual amino acids that make up proteins, categorizing them based on properties like charge, size, hydrophobicity, and whether they contain aromatic, hydroxyl, sulfur, or acidic/basic functional groups. It discusses how these various amino acid properties and interactions determine protein structure and function.
Amino acids can be classified into five main classes based on the properties of their R groups, particularly their polarity or tendency to interact with water at biological pH. The classes are nonpolar aliphatic, aromatic, polar uncharged, positively charged (basic), and negatively charged (acidic). The nonpolar aliphatic amino acids like alanine and valine stabilize protein structure through hydrophobic interactions. Positively charged amino acids like lysine and arginine have ionizable side chains that are positively charged at pH 7. Negatively charged amino acids aspartate and glutamate have side chains with a net negative charge at biological pH.
Properties of amino acid side chains report ni ladyAya Chavez
The document discusses the different classes of amino acid side chains. The 20 common amino acids can be grouped based on the chemical properties of their side chains. The main classes discussed are amino acids with aliphatic/hydrophobic side chains like glycine and alanine; hydroxyl- or sulfur-containing side chains like serine and cysteine; aromatic side chains like phenylalanine and tyrosine; basic side chains like histidine and lysine; and acidic side chains like aspartic acid and glutamic acid. The different properties of the side chains influence how hydrophobic or hydrophilic the amino acids are and where they are located in protein structures.
Properties of amino acid side chains report ni ladyAya Chavez
The document discusses the different classes of amino acid side chains. The 20 common amino acids can be grouped based on the chemical properties of their side chains. The main classes discussed are amino acids with aliphatic/hydrophobic side chains like glycine and alanine; hydroxyl- or sulfur-containing side chains like serine and cysteine; aromatic side chains like phenylalanine and tyrosine; basic side chains like histidine and lysine; and acidic side chains like aspartic acid and glutamic acid. The different properties of the side chains influence how hydrophilic or hydrophobic the amino acids are and where they are generally found within protein structures.
This document discusses proteins and amino acids. It begins by defining proteins as polymers of amino acids, which are the building blocks of proteins. There are 20 standard amino acids that make up proteins. The document then classifies and describes the properties of amino acids and the different types of protein structures from primary to quaternary structure. It notes the various functions of proteins, including as enzymes, hormones, antibodies, and structural components. The document concludes by discussing plasma proteins, their functions in transport and maintaining pH balance, and the major plasma proteins of albumin and globulins.
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.
Amino acids are the building blocks of proteins. They contain carbon, hydrogen, oxygen, nitrogen and a distinctive side chain. There are 20 common amino acids that serve as monomers for protein synthesis. Amino acids differ in their side chains, which influence solubility. The general structure includes an amino group, carboxyl group, hydrogen and R group. Amino acids form proteins through peptide bonds between their amino and carboxyl groups. Proteins have primary, secondary, tertiary and quaternary levels of structure determined by amino acid sequence and bonding.
- Amino acids are the building blocks of proteins and contain an amino group, carboxyl group, hydrogen atom, and side chain bonded to an alpha carbon.
- There are 20 standard amino acids that vary in properties based on their side chains. Phenylalanine, methionine, and tryptophan are hydrophobic while cysteine forms disulfide bridges.
- Proteins are made of chains of amino acids that can form different structures like fibrous or globular proteins depending on their shape and solubility.
The document discusses protein structure at multiple levels of organization. It describes the 20 amino acids that make up proteins and how they can be categorized based on properties like size and affinity for water. It then explains how amino acids join together through peptide bonds to form the primary structure of a protein as a linear sequence. Secondary structures like alpha helices and beta sheets involve hydrogen bonding between amino acids to create regular local structures. Tertiary structure refers to the overall 3D shape formed by packing and arrangement of secondary structures. There are two main types of tertiary structure - globular proteins that are soluble and membrane proteins that exist in cell membranes.
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
Amino and carboxylic acid functional groups can both be found in organic compounds known as amino acids. Although there are more than 500 amino acids in nature, the alpha-amino acids, which make up proteins, are by far the most significant. The genetic code of every living thing contains just 22 alpha glucosamine.
This document discusses amino acids, peptides, and proteins. It begins by defining them as monomers (amino acids), polymers of a few monomers (peptides), and polymers of many monomers (proteins). It then covers the structures and properties of amino acids, including the 20 that are found in proteins. Peptide bond formation is explained as linking amino acids together. Various proteins are classified and examples given, including simple proteins like albumins and globulins, and structural proteins like keratins, collagens, and elastins. The roles and importance of proteins in the body are also summarized.
Proteins have four levels of structural organization: primary, secondary, tertiary, and quaternary. The primary structure refers to the linear sequence of amino acids in the polypeptide chain. Secondary structure involves local folding patterns like alpha helices and beta sheets. Tertiary structure describes the overall 3D shape of a single polypeptide chain. Quaternary structure is the 3D structure formed by the assembly of multiple polypeptide subunits. The structures at each level are stabilized by interactions between the R groups of amino acids in the chain.
Proteins are composed of amino acids and have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves local folding into patterns like alpha helices and beta sheets. Tertiary structure is the overall three-dimensional shape formed by interactions between different parts of the polypeptide chain. Quaternary structure refers to the shape of proteins with multiple polypeptide subunits. Proteins perform many important functions in the body as enzymes, antibodies, hormones, and structural components.
The document summarizes key aspects of amino acids and protein structure in 3 paragraphs or less:
Amino acids are the building blocks of proteins. They contain common structural features and exist in L- and D-forms. In proteins, amino acids are exclusively in the L-conformation. Amino acids are classified based on the properties of their side chains into nonpolar, aromatic, polar, positively charged, and negatively charged categories.
Protein structure is hierarchical, progressing from primary to secondary, tertiary, and quaternary levels. The primary structure is the amino acid sequence. Secondary structures include alpha helices, beta sheets, and turns formed by hydrogen bonding. Tertiary structure refers to the overall 3
Effect of physical parameters on the properties of PROTEINSNeeraj Kumar
Proteins are composed of chains of amino acids that are linked together by peptide bonds. The amino acid composition determines a protein's properties. There are four levels of protein structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure describes the three-dimensional folding of the polypeptide chain. Quaternary structure results from interactions between subunits in multimeric proteins.
The document discusses the structure and functions of proteins. It begins by defining alpha-amino acids as compounds containing an amino group and a carboxylic acid group. It then describes the characteristic properties of amino acids, including their zwitterion structure and buffering properties. The document explains how amino acids undergo condensation reactions to form polypeptides via peptide bonds. It details the primary, secondary, tertiary, and quaternary structure of proteins. Finally, it lists the major functions of proteins in the body, such as serving as enzymes, hormones, antibodies, and structural components.
Dystrophin is a high molecular weight cytoskeletal protein that localizes to the cytoplasmic face of the sarcolemma. It has four domains - an actin binding domain, a central rod domain composed of spectrin-like repeats, a cysteine-rich domain, and a carboxy-terminal domain. Dystrophin forms the dystrophin-glycoprotein complex with other proteins like dystroglycans and sarcoglycans to connect the actin cytoskeleton to the extracellular matrix. Mutations in dystrophin cause Duchenne/Becker muscular dystrophy by disrupting this connection and leading to muscle degeneration.
The document discusses body fluids, cerebrospinal fluid (CSF), and distinguishing between transudates and exudates. Key points include:
- CSF is produced by the choroid plexus at a rate of 500 ml per day and acts as a cushion and lubricant for the brain. Analysis of CSF provides information about infections and CNS disorders.
- Transudates have a low protein content and occur due to decreased plasma proteins or increased venous pressure. Exudates have a high protein content and occur due to inflammation or tissue damage.
- CSF analysis involves examination of appearance, chemical properties like glucose and protein levels, cell counts, and microbiological tests to identify infections. Abnormal results can indicate conditions
Enzymes are protein catalysts found in cells and tissues. They are responsible for chemical reactions in the body and can be detected in serum to diagnose diseases. Increased enzyme levels in serum may indicate tissue damage or certain disease states. Common enzymes measured include alkaline phosphatase, acid phosphatase, amylase, lipase, SGPT and SGOT which can help diagnose diseases of the bones, prostate, pancreas and liver. Enzymes function as biological catalysts by lowering the activation energy of reactions and increasing their rates without being consumed in the process. They are highly specific and their activity can be affected by factors like pH, temperature, substrate and inhibitor concentrations.
The document discusses abnormalities of white blood cells, including quantitative abnormalities like leukocytosis and leukopenia as well as qualitative abnormalities involving the nucleus or cytoplasm of white blood cells. Some examples of qualitative abnormalities discussed include Pelger-Huet anomaly, Chediak-Steinbrinck-Higashi syndrome, and Auer rods. The types of white blood cells are described along with causes of conditions like neutrophilia, eosinophilia, lymphocytosis, and monocytosis. Inherited and acquired morphological and functional abnormalities of white blood cells are also summarized.
This document summarizes the three main stages of cellular respiration: glycolysis, the Krebs cycle, and the electron transport chain.
[1] Glycolysis occurs in the cytoplasm and breaks down glucose into pyruvate, while the Krebs cycle in the mitochondrial matrix further breaks down pyruvate into carbon dioxide. [2] Several steps in glycolysis and the Krebs cycle pass electrons to NAD+, which is then used by the electron transport chain in the mitochondria. [3] The electron transport chain uses a series of electron carriers and pumps hydrogen ions across the inner mitochondrial membrane. This proton gradient is then used by ATP synthase to produce ATP through oxidative phosphorylation.
This document provides information on methods for performing a complete blood count (CBC), including white blood cell (WBC) count, corrected WBC count, and differential leukocyte count (DLC). The WBC count involves using a counting chamber, pipettes, and diluting fluids to count WBCs under a microscope. The DLC involves making a blood smear, staining it, counting different types of WBCs, and reporting results as relative or absolute counts. Normal ranges are provided for WBC subtype percentages and counts.
The document discusses various methodologies for analyzing red blood cells (RBCs). It describes the erythrocyte sedimentation rate (ESR) test, which measures how quickly RBCs settle in plasma, and lists several methods for performing the test including the Wintrobe and Westergren methods. It also covers the osmotic fragility test, which examines RBC stability in hypotonic solutions, and erythrocyte indices, which provide information about average RBC size, hemoglobin content, and concentration by calculating mean corpuscular volume, hemoglobin, and hemoglobin concentration.
The MHC encodes antigen presenting molecules that display peptide fragments to T cells to initiate immune responses. It contains three regions - Class I MHC presents intracellular peptides to CD8+ T cells, Class II MHC presents extracellular peptides to CD4+ T cells, and Class III MHC encodes complement proteins. MHC molecules are highly polymorphic and individuals inherit multiple alleles from each parent. This polymorphism allows presentation of a wide range of peptides and enhances immune responses against pathogens. MHC matching is important for transplantation, as mismatch can lead to graft rejection through T cell recognition of foreign MHC.
Brucella species are small, gram-negative bacteria that can cause brucellosis in humans and animals. They infect a variety of animal hosts and are transmitted to humans through contact with infected animals or consumption of unpasteurized dairy. In humans, Brucella bacteria localize in tissues like lymph nodes, liver, and bone, causing non-specific symptoms like fever, sweats, and joint pain. Diagnosis involves culture of the bacteria from blood or tissues or detection of antibodies in serum. Treatment requires a combination of antibiotics for an extended duration.
This document discusses Treponema pallidum, the spirochete bacteria that causes syphilis. It describes the morphology and pathogenic species of Treponema, focusing on T. pallidum. The stages of syphilis and correlation with test results are outlined. Antibodies produced during syphilis infection and their development are explained. Treatment of syphilis and its effects on test results are also summarized. Related diseases caused by other Treponema species like yaws are briefly mentioned.
This document describes various abnormalities that can be seen in red blood cells during a blood smear examination. It defines different types of anisocytosis (variation in red blood cell size), anisochromia (variation in hemoglobin concentration), and abnormal red blood cell shapes that may indicate underlying hematological disorders. Various intracellular inclusions and remnants such as Howell-Jolly bodies, Heinz bodies, and Pappenheimer bodies are also described.
How to Build a Module in Odoo 17 Using the Scaffold MethodCeline George
Odoo provides an option for creating a module by using a single line command. By using this command the user can make a whole structure of a module. It is very easy for a beginner to make a module. There is no need to make each file manually. This slide will show how to create a module using the scaffold method.
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.
Executive Directors Chat Leveraging AI for Diversity, Equity, and InclusionTechSoup
Let’s explore the intersection of technology and equity in the final session of our DEI series. Discover how AI tools, like ChatGPT, can be used to support and enhance your nonprofit's DEI initiatives. Participants will gain insights into practical AI applications and get tips for leveraging technology to advance their DEI goals.
Introduction to AI for Nonprofits with Tapp NetworkTechSoup
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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.
it describes the bony anatomy including the femoral head , acetabulum, labrum . also discusses the capsule , ligaments . muscle that act on the hip joint and the range of motion are outlined. factors affecting hip joint stability and weight transmission through the joint are summarized.
Macroeconomics- Movie Location
This will be used as part of your Personal Professional Portfolio once graded.
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Prepare a presentation or a paper using research, basic comparative analysis, data organization and application of economic information. You will make an informed assessment of an economic climate outside of the United States to accomplish an entertainment industry objective.
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Thinking of getting a dog? Be aware that breeds like Pit Bulls, Rottweilers, and German Shepherds can be loyal and dangerous. Proper training and socialization are crucial to preventing aggressive behaviors. Ensure safety by understanding their needs and always supervising interactions. Stay safe, and enjoy your furry friends!
3. BASIC STRUCTURES
An amino acid contains:
a central carbon bonded to a carboxyl group (-COOH),
an amino group (NH2), an
R-group, and
a hydrogen.
The R-group is what varies between the 20 amino acids and
gives them unique characteristics.
The covalent bonds between amino acids are called peptide
bonds.
It is a bond between the carboxyl group of one amino acid
and the amino group of another amino acid.
4. Abbre
Full Name Side chain type Remarks
v.
Very abundant and versatile. It behaves fairly
neutrally and can be located in both hydrophilic
A Ala Alanine hydrophobic
regions on the outside of the protein and
hydrophobic interior areas.
The sulfur atom binds readily to heavy metal ions.
Under oxidizing conditions, two cysteines can be
joined together by a disulfide bond to form the amino
acid cystine. When cystines are components of a
protein, they enforce tertiary structure and makes
hydrophobic (Nagano, the protein more resistant to unfolding and
C Cys Cysteine
1999) denaturation; disulfide bridges are therefore
common in proteins that have to function in harsh
environments, digestive enzymes (e.g., pepsin and
chymotrypsin), structural proteins (e.g., keratin), and
proteins too small to hold their shape on their own
(eg. insulin).
Behaves similarly to glutamic acid. Carries a
hydrophilic acidic group with strong negative charge.
Aspartic Usually is located on the outer surface of the protein,
D Asp acidic
acid making it water-soluble. Binds to positively-charged
molecules and ions, often used in enzymes to fix the
5. Side chain
Abbrev. Full Name Remarks
type
Phenylalanine, tyrosine, and tryptophan contain large rigid
aromatic group on the side chain. These are the biggest
Phenylala
*F Phe hydrophobic amino acids. Like isoleucine, leucine and valine, they are
nine
hydrophobic and tend to orient towards the interior of the
folded protein molecule.
Because of the two hydrogen atoms at the α carbon, glycine is
not optically active. It is the smallest amino acid, rotates easily,
G Gly Glycine hydrophobic
and adds flexibility to the protein chain. It is able to fit into the
tightest spaces (e.g., the triple helix of collagen).
In even slightly acidic conditions, protonation of the nitrogen
occurs, changing the properties of histidine and the
polypeptide as a whole. It is used by many proteins as a
*H His Histidine basic regulatory mechanism, changing the conformation and
behavior of the polypeptide in acidic regions such as the late
endosome or lysosome, enforcing conformation change in
enzymes.
Isoleucine, leucine and valine have large aliphatic hydrophobic
side chains. Their molecules are rigid, and their mutual
hydrophobic interactions are important for the correct folding
*I Ile Isoleucine hydrophobic
of proteins, as these chains tend to be located inside of the
protein molecule.
6. Side chain
Abbrev. Full Name Remarks
type
Behaves similarly to arginine. Contains a long flexible side-
chain with a positively-charged end. The flexibility of the chain
makes lysine and arginine suitable for binding to molecules
with many negative charges on their surfaces. (e.g., DNA-
*K Lys Lysine basic
binding proteins have their active regions rich with arginine
and lysine.) The strong charge makes these two amino acids
prone to be located on the outer hydrophilic surfaces of the
proteins.
*L Leu Leucine hydrophobic Behaves similar to isoleucine and valine.
Always the first amino acid to be incorporated into a protein;
sometimes removed after translation. Like cysteine, it
contains sulfur, but with a methyl group instead of hydrogen.
*M Met Methionine hydrophobic
This methyl group can be activated, and is used in many
reactions where a new carbon atom is being added to
another molecule.
N Asn Asparagine hydrophilic Neutralized version of aspartic acid.
7. Side chain
Abbrev. Full Name Remarks
type
Contains an unusual ring to the N-end amine group, which
forces the CO-NH amide sequence into a fixed conformation.
Can disrupt protein folding structures like α helix or β sheet,
P Pro Proline hydrophobic
forcing the desired kink in the protein chain. Common in
collagen, where it undergoes a posttranslational modification
to hydroxyproline. Uncommon elsewhere.
Neutralized version of glutamic acid. Used in proteins and as
Q Gln Glutamine hydrophilic
a storage for ammonia.
*R Arg Arginine Basic Functionally similar to lysine.
Serine and threonine have a short group ended with a
hydroxyl group. Its hydrogen is easy to remove, so serine
S Ser Serine Hydrophilic and threonine often act as hydrogen donors in enzymes. Both
are very hydrophilic, therefore the outer regions of soluble
proteins tend to be rich with them.
8. Side chain
Abbrev. Full Name Remarks
type
*T Thr Threonine hydrophilic Behaves similarly to serine.
Behaves similarly to isoleucine and leucine.
*V Val Valine hydrophobic
See isoleucine.
Behaves similarly to phenylalanine and
*W Trp Tryptophan hydrophobic tyrosine (see phenylalanine). Precursor of
serotonin.
Behaves similarly to phenylalanine and
Y Tyr Tyrosine hydrophobic tryptophan (see phenylalanine). Precursor of
melanin, epinephrine, and thyroid hormones.
10. GENERALITIES - NEUTRAL
A. Aliphatic Hydroxy Amino Acids – they contain
OH group in the side chains
1. Glycine (Gly) (G) – alpha–
amino acetic acid 6. Serine (Ser) (S) or alpha – amino
β – hydroxy propionic acid
2. Alanine (Ala) (A) – alpha – 7. Threonine (Thr) (T) or alpha –
amino propionic acid amino β – hydroxybutyric acid
3. Valine (Val) (V) – alpha–
amino – iso – valeric acid
4. Leucine (Leu) (L) – alpha –
amino – iso – caproic acid
5. Isoleucine (Ile) (l) – alpha –
amino – B – methyl valeric
acid
Above = Simple monoamino
monocarboxylic acids
11. GENERALITIES
B. Aromatic C. Heterocyclic AA
8. Phenylalanine (Phe) (F) 10. Tryptophan (Trp) (W) –
or alpha – amino – β – alpha – amino β – 3 – indole
phenyl propionic acid propionic
- often considered
9. Tyrosine (Tyr) (y) or as aromatic AA since it has
parahydroxy aromatic ring in its structure.
phenylalanine or alpha – 11. Histidine (His) (H) –
amino β – parahydroxy alpha – amino – β -
phenylpropionic acid imidazole propionic acid
Histidine is basic in solution
on account of the imidazole
ring and often considered as
Basic AA
12. GENERALITIES
D. Imino Acids E. „S‟ containing Amino Acids
12. Proline (Pro) (P) or - contains 2 sulfur containing
AA
Pyrrolidone – 2 – carboxylic
Acid
14. Cysteine (Cys) (C) or alpha –
13. Hydroxyproline (Hyp) or 4 – amino – β – mercaptopropionic
Hydroxy pyrrolidone – 2 – acid
carboxylic acid S – S linkage is called a
Disulfide bridge
Proline & Hydroxyproline do 15. Methionine (Met) (M) or alpha
not have a free _NH2 group but – amino y – methylthio - - butyric
only a basic pyrrolidone ring in acid
which the Nitrogen of the Imino
group is in ring but can still
function in the formation of
peptides.
Are called Imino Acids.
13. GENERALITIES - ACIDIC
II. Acidic AA
- AA with 2 _COOH groups and 1 _NH2 group
- monoaminodicarboxylic Acids
16. Aspartic Acid (Asp) (P) or alpha – amino succinic acid
Asparagine (Asn) (N) or delta amide of alpha – amino
succinic acid
17. Glutamic Acid (Glu) (E) or alpha aminoglutaric acid
Glutamine (Gln) (Q) – amide of glutamic acid or 8 –
amide of alpha – amino glutaric acid
14. GENERALITIES - BASIC
III. Basic AA
- AA with 1 – COOH group and 2 – NH2
groups
- Diamino monocarboxylic acids
18. Arginine (Arg) (R) or alpha – amino – 8 – guanidino
- valeric acid
19. Lysine (Lys) (K) or alpha – E diamino
8 – hydroxy - - valeric acid
As already mentioned Histidine – is also classified as
Basic AA
15. GENERALITIES
Classificationof Amino Acids
based on polarity
of the R group:
• 4 groups
• Polarity reflects the
functional role
of AA in protein structure
16. GENERALITIES
1. Non-polar AA
• hydrophobic (water hating)
• No charge on the ‘R’ group
• Examples are:
Alanine Methionine
Leucine
Phenylalanine
Isoleucine
Tryptophan
17. GENERALITIES
2. Polar AA with (+) ‘R’ group
• carries (+) charge
• Examples:
Histidine Arginine
Lysine
3. Polar AA with (-) ‘R’ group
• carries (-) charge
• Examples:
Glutamic Acid
Aspartic Acid
18. GENERALITIES
4. Polar AA with no charge
on ‘R’ group
• no charge on the ‘R’ group
• possess groups hydroxyl
sulfhydryl
amide
• participate in hydrogen bonding of
• protein structure
• Examples:
Asparagine Glycine Cysteine
Tyrosine Serine Threonine
19. GENERALITIES
Zwitterion or dipolar ion:
Zwitter
from German word – means
“hybrid”
Zwitter ion (or dipolar ion)
a hybrid molecule containing
(+) and (-) ionic groups
20. GENERALITIES
AA rarely exist in a neutral form with free
carboxylic (-COOH) and free Amino (-NH2)
groups
Strongly acidic pH (low pH) AA (+)
charged (cation)
Strongly alkaline pH (high pH) AA (-)
charged (anion)
Each AA has a characteristic pH (e.g. Leucine,
pH – 6.0), at which it carries both (+) and (-)
charges and exist as zwitterion
21. GENERALITIES
Isoelectric pH (symbol pI)
the pH at which a molecule exists as a
Zwitterion or dipolar ion and carries
no net charge
Molecule is electrically neutral
22. GENERALITIES
Tryptophan
Histidine Arginine Leucine
Valine
Phenylalanine PVT TIM HALL Lysine
Threonine Methionine
Isoleucine
Essential Amino Acids
23. Essential Amino Acids (Body cannot make these amino acids, they must come
from food or amino acid supplements.)
Min.
Dail Acid
y Base # of pathways - One Generate Works
Amino Acid Sym Abbr mg Neu. Pathway s With Augments
1 - threonine -->
1 Isoleucine* I Ile 10 n - - muscles
isoleucine
blood,
1 - keto-isovalerate --
2 Leucine* L Leu 14 n - - muscle,
> leucine
hormone
herpes,
3 Lysine K Lys 12 B 2 - asparate --> lysine - calcium
triglycerides
7 - homoserine --> seleniu hair, skin,
4 Methionine M Met 13 n cysteine
methionine m, zinc chelator
Phenylalanin 3 - chorismate -->
5 F Phe 14 n tyrosine B6 depression
e phenylalanine
collagen,
3 - aspartate --> glycine,
6 Threonine T Thr 7 N - tooth
threonine serine
enamel
1 - chorismate --> niacin,
7 Tryptophan W Trp 3.5 n - depression
tryptophan seratonin
8 Valine* V Val 10 n 1 - pyruvate --> valine - - muscles
Food Sources: Fish - meat - poultry - cottage cheese - peanuts - lentils
A= acid, B= base, N= Neutral, n= non-polar
24. Non-Essential Amino Acids (The body can make these amino acids from the above essential amino
acids.)
Min. Acid
Daily Base # of pathways - One
Amino Acid Sym. Abbr mg. Neu. Pathway Generates Works With Augments
4 - valine pyruvate -->
1 Alanine A Ala - n - - -
alanine
immune,
polyamines,
2 Arginine* R Arg - B 4 - citrulline --> arginine zinc (lysine) healing,
creatine
muscles
3 Asparagine N Asn - N 3 - asparate and ammonia - - CNS
Aspartic
4 D Asp - A 3 - glutamate --> aspartate - - CNS, brain
Acid
homocysteine
5 Cysteine C Cys - N 4 - serine --> cysteine B6, Vit.E skin, hair
, taurine
Glutamic 3 - ketoglutarate --> glutamine,
6 E Glu - A B6 brain
Acid glutamate GABA
7 Glutamine Q Gln - N 2 - glutamate --> glutamine - - brain
GABA,
8 Glycine G Gly - N 2 - serine --> glycine glutathione body protein
taurine
blood, allergy,
9 Histidine* H His - B 1 - histidinol --> histidine histamine -
sex
hydroxyprolin collagen,
10 Proline P Pro - n 4 - l-glutamine --> proline Vitamin C
e elastin
1 - phosphoglycerate --> cysteine,
11 Serine S Ser - N choline blood sugar
serine glycine
2 - phenylalanine --> thyroxin,
12 Tyrosine Y Tyr - N B6 thyroid
tyrosine melanin
* = These are Essential for infants, since their bodies cannot produce them yet.
25. Other Amino Acid Factors
Lysine,
carnitine --> fat
- Carnitine - Car - - methionin Vitamin C
butyrobetaine --> metabolism
e
argenine --> citrulline
- Citrulline - Cit - - Ornithine zinc urea cycle
--> ornithine
Hydroxy Hy proline -->
- - - - - Vitamin C collagen
proline p hydroxyproline
Or argenine --> citrulline
- Ornithine - - - - - urea cycle
n --> ornithine
methionine --> GABA,
- Taurine - Tau - - B6 heart, bile
cysteine --> taurine glycine
The above are precursors for, or important products of, the 20 "true" amino acids
listed above.
26. AMINO ACID SYNTHESIS
ALL ARE SYNTHESIZED FROM COMMON
METABOLIC INTERMEDIATES
NON-ESSENTIAL
Transamination of -KETOACIDS that are
available as common intermediates
All except tyrosine are derived from one of the
following common intermediates: pyruvate,
oxalacetate, -KG, 3-phosphoglycerate
ESSENTIAL
Their -KETOACIDS are not common
intermediates (Enzymes needed to form them
are lacking)
27. Amino Acids Glucogenic Glucogenic and Ketogenic
A
Ketogenic
m Non-Essential Alanine Tyroxine
i AA Asparagine
n
o Aspartate
A Cysteine
c Glutamate
i
d Glutamine
M Glycine
e Proline
t
a
Serine
b
o Essential AA Arginine Isoleucine Leucine
l
Histidine Phenylalanine Lysine
i
s Methionine Tryptophan
m Threonine
Valine
Glucogenic – amino acids that give rise to pyruvate and
citric acid cycle intermediates that can be turned into
glucose
Ketogenic – amino acids that give rise to acetoacetate and
29. TYROSINEMIA
DEFECTIVE PROCESS: AMINO ACID TRANSPORT – EXCRETION
OF TYROSINE AND TRYPTOPHAN CATABOLITES IN URINE
DEFECTIVE ENZYME:
• TYROSINE AMINOTRANSFERASE (II);
• 4-HYDROXY-PHENYLPYRUVATE OXIDASE (III);
• FUMARYLACETOACETATE HYDROLASE (I)
30. ALKAPTONURIA
DEFECTIVE PROCESS: TYROSINE
DEGRADATION
DEFECTIVE ENZYME: HOMOGENTISATE-
1,2-DIOXYGENASE
• Original “inborn error of metabolism
• Darkening of urine at long standing
• OCHRONOSIS – generalized pigmentation of
tissues and arthritislike degeneration
31. PHENYLKETONURIA
DEFECTIVE PROCESS: CONVERSION OF
PHENYLALANINE TO TYROSINE
DEFECTIVE ENZYME: PHENYLALANINE
HYDROXYLASE (Phenylalanine-4-mono-oxygenase)
An autosomal recessive trait – urine has a musty
odor
Compounds seen in both urine and blood:
Phenylpyruvic acid – primary catabolite
Phenyllactic acid – product of deaminzation
Phenylacetylglutamine – produced from oxidation of
phenylpyruvic acid
32. PHENYLKETONURIA
NOT RESPONSIVE TO DIET: DEFICIENCY OF ENZYME S NEEDED FOR
THE REGENERATION AND SYNTHESIS OF TETRAHYDROBIOPTERIN
(BH4)
• High phenylalanine and deficiency of production of neurotransmitters
from tyrosine and tryptophan
• Administration of L-dopa and 5-OH tryptophan
SCREENING: GUTHRIE BACTERIAL INHIBITION ASSAY – B. subtilis +
β2-thienylalanine
• Semi-qualitative method: phenylalanine >2-4 mg/dL will result to
bacterial growth indicative of a POS (+) result
• Microfluorometric assay – based on the fluorescence complex formed of
phenylalanine-ninhydrin copper in the presence of dipeptides (L-leucyl-L-
alanine)
• Quantitative method: filter paper is pretreated with trichloroacetic acid
added with ninhydrin, succinate and leucylalanine in the presence of
copper tartrate and read at excitation and emission wavelengths of
360nm and 530nm
HPLC – reference method (1.2 -3.4 mg/dL)
33. MAPLE SYRUP DISEASE
DEFECTIVE PROCESS: METABOLISM OF THREE ESSENTIAL
BRANCHED-CHAINAMINO ACIDS (LEUCINE, ISOLEUCINE AND VALINE)
DEFECTIVE ENZYME: BRANCHED CHAIN α-KETO ACID
DECARBOXYLASE COMPLEX
• Burnt sugar odor of urine, breath and skin
• Screening: Modified Guthrie test – metabolic inhibitor of B. subtilis which is
4-azaleucine is impregnated in the medium
• POS (+) for MSUD = bacterial growth
• Microfluorometric assay using leucine dehydrogenase
• Filter paper specimen is treated with methanol and acetone to denature
hemoglobin
• The NADH fluorescence produced is measured at 450nm; excitation
wavelength at 360nm
• Confirmed diagnosis is based on finding increased plasma and urinary levels
of the three branched-chain amino acids and their ketoacids with LEUCINE
(highest: above 4mg/dL)
• Prenatal diagnosis: measuring decarboxylase enzyme concentration in cells
cultured from amniotic fluid
34. CYSTINURIA
DEFECTIVE PROCESS: AMINO ACID TRANSPORT
SYSTEM RATHER THAN A METABOLIC ENZYME
DEFICIENCY
• 20 – 30 fold increase in the urinary excretion of cystine
as a result of genetic defect in the renal resorptive
mechanism
• Other amino acids excreted: ornithine, lysine and
arginine
• Cystine being relatively insoluble and once
accumulated will tend to precipitate in the kidney
tubules forming calculi
• Remedy: high fluid intake and alkalinizing the urine:
penicillin
• Diagnosis: Cyanide-nitroprusside (red-purple color)
35. ARGININOSUCCINIC ACIDURIA AND
CITRULLINEMIA PROCESS: UREA CYCLE
DEFECTIVE
DEFECTIVE ENZYME: ARGININOSUCCINIC
ACID LYASE
• Decrease in activity of ASA synthetase
Citrullinemia
• Citrulline is elevated in MS/MS
• Argininosuccinic aciduria – milder
elevations
• Citrullinemia – dramatic elevations
• * Ornithine and arginine are seen
increased in older infants
36. ISOVALERIC ACIDEMIA
DEFECTIVE PROCESS: DEGRATIVE
PATHWAY OF LEUCINE
DEFICIENCY ENZYME: ISOVALERYL-CoA
DEHYDROGENASE
• “Sweaty feet” odor urine
• Elevations of glycine conjugate: isovaleric
acid and isovalerylglycine
39. FUNCTIONS OF PROTEINS
1. Enzymatic catalysis
2. Transport and storage
3. Coordinated motion
responsible for movements in the body
(muscles)
4. Mechanical support
support of body - bones and muscles
5. Generation and transmission of impulses
6. Control of growth and differentiation
AA - simplest form of proteins
20 AA
40. CHARACTERISTICS OF PROTEINS
1. Have more members
2. Fundamental component of protoplasm
3. Elements in protein
C, H, O, N (I & Fe)
4. Proteins are considered macromolecules,
composed of a number of AA joined together by
peptide bond or linkage
5. Only foodstuff when absent in the diet will
cause death
6. Utilize in the body for growth
41. PROTEIN METABOLISM
GASTRIC
• Digestion of protein begins in the stomach
where the enzyme pepsin is secreted by the
chief cells as proenzyme or zymogen
(inactive form)
• Pesinogen – activated by HCL secreted by
the parietal cells
• By autoactivation – pepsin itself stimulates
its own activation
42. PROTEIN METABOLISM
PANCREATIC
• Once protein reaches the duedenum, exocrine
pancreatic secretion: trypsin,chymotrypsin,
elastase and carboxypeptidase in their inactive
forms are release
• Endopeptidase – cleave protein in the
internal sites
• Exopeptidase – cleave one amino acid
from the carboxyl terminus of the
polypeptide
Secretin stimulates the pancreas to
produce a protein-free electrolyte solution
rich in bicarbonates
43. PROTEIN METABOLISM
INTESTINAL
• This mediated by peptidase produced by the
mucosal cells
• Amino peptidases and dipeptidases hydrolyze the
residual peptides
• The end products of protein digestion are amino
acids and some short peptides
44. AMINO ACID POOL
Primarily for the Also for the synthesis of
synthesis of body nonprotein nitrogen-
proteins: containing compounds
• Plasma • Purines
• Intracellular proteins • Pyrimidines
• Structural proteins • Creatine
• Porphyrins
• Histamines
46. DETERMINATION OF PROTEIN NITROGEN
KJELDAHL
• Reference (standard) method for the determination
of protein concentration
• Liberation the nitrogen content from proteins is
measured by oxidation with heat at 350oC and
strong sulfuric acid
• Catalysts used during the digestion: copper sulfate,
mercuric sulfate or selenium oxychloride
• Nitrogen then is converted to ammonium ion
• Separated from the digestant by steam
distillation
• Ammonium ion is liberated and are measured
by titration with an alkali, Nesslerization or
47. NESSLERIZATION
• Liberation of ammonium ions with Nessler‟s reagent –
double iodide of potassium and mercury dimercuric
ammonium iodide (yellow to orange brown product
• Colloidal stabilizer: gum ghatti
BERTHELOT
• Idophenol reaction
• Ammonia is allowed to react with alkaline hypochlorite to
form indophenol blue solution
• Catalyst: sodium nitroprusside
48. BIURET REACTION
Based on the ability of the peptide bonds to react with
copper ions to form purple “biuret” complex
Biuret reagent contains:
• Copper sulfate – biuret formation
• Sodium hydroxide
• Rochelle salt (potassium sodium tartrate) – stabilizes
the copper sulfate
• Potassium iodide – keeps copper ions in cupric state
• The purple complex is measure at 540 – 560 nm
Total proteins – measure by allowing to react with the
biuret reagent
“Salting-out process” – precipitation of globulins with 22-
26% sodium sulfate to get the albumin content
49. FOLIN-CIOCALTEAU METHOD
based on the ability of phosphotungstomolybdic
acid (phenol reagent or Folin-Ciocalteau‟s reagent)
to oxidize the phenolic structures of the amino
acids tyrosine, phenylalanine, tryptophan and
histidine.
50. LOWRY PROTEIN ASSAY
• Uses biuret method followed by the
Folin-Ciocalteau‟s method
• Color obtained is enhance and provide a
more sensitive method
• Consistently obtained accurate protein
determination
51. COOMASIE BRILLIANT BLUE DYE
• Free from interferences
• It can detect proteins as low as 1 ug in
concentration
52. NINHYDRIN REACTION
• Used to detect peptides and amino acids
after paper chromatography
• Violet color formation upon reaction to
ninhydrin (tri-keto-hydrindine hydrate
and amines
• Results are comparable to Coomasie
dye method
53. REFRACTOMETRY
• Measuring refractive index of serum
• Accurate levels are obtained at protein
concentrations greater than 2.5 g/dL
54. SPECIFIC GRAVITY
• Copper sulfate standards with known
specific gravity
• Measurement of hemoglobin
55. TURBIDIMETRY
• Measures total proteins and globulins
in urine and CSF
• Proteins are precipitated by
sulfosalicylic acids, trichloroacetic
acid, acetic acid-potassium
ferricyanide solution
56. UV ABSORPTION METHOD
• Proteins absorb UV light at 280 nm
• Mostly due to the presence of tryptophan,
phenylalanine and tyrosine
• Quantifies protein in the range of 0.5 to 1.5
mg/dL
57. ELECTROPHORESIS
Sodium dodecyl sulfate polyacrilamide gel
electrophoresis
• Separates protein according to molecular weight
and isoelectric focusing which separates proteins
on the basis of isoelectric poins
• After separation, proteins are quantified by densitometry
(preferred method and by elution and spectrophotometry
Qualitative characterization of proteins may be stained
with appropriate dyes:
1. Coomasie brilliant blue
2. Ponceau S
3. Amido black
4. Silver staining - most sensitive and measures proteins
in nanogram concentration
59. PLASMA PROTEIN
PRE-ALBUMIN
• Migrates faster than albumin toward the
anode
• Has the ability to bind with thyroxine (TBPA)
and complex with vitamin A
• Very rich with tryptophan
• Marker of nutritional status
• Crosses the plancenta
60. ALBUMIN
• Single most abundant protein in normal plasma
• About 2/3 of the total plasma proteins
• Regulates intravascular oncotic pressure
• Loss of albumin is seen in ascites, protein
losing nephropathy and protein losing
enteropathy
• Seen in peripheral edema
Functions of albumin:
1. Regulation of oncotic pressure
2. Amino acid reservoir
3. Transport of small molecules
61. ALBUMIN
• Bounded by thyroxine, bilirubin, penicillin,
cortisol, estrogen and free fatty acids
• Calcium and magnesium
• Analbuminemia – absence of albumin in
the blood
• Bisalbuminemia – two separated albumin
bands after electrophoresis
62. ALPHA1-ANTITRYPSIN
• Major component of the alpha1-globulin
fraction
• Acts as protease inhibitor
• Combines with and inactivates trypsin and
elastase
• In lungs, elastase is released by the
neutrophils during inflammatory conditions
to combat the invading microorganisms
• Deficiency will result to emphysema
• Also an intrinsic factor in homeostatic
mechanism modulating endogenous
proteolysis with the body
63. ALPHA2-MACROGLOBULIN
• one of the largest non-immunoglobulin
proteins in the plasma
• Rises tenfold or more in nephrotic
syndrome when other low molecular
weight proteins are lost
• In nephrotic syndrome, the levels of
alpha2-macroglobulin may be equal to or
greater than that of albumin (2-3 g/dL)
64. HAPTOGLOBIN
• Haptoglobin migrates in the alpha2-region
• Combines with hemoglobin released by lysis of red
blood cells in order to preserve body iron and
protein stores
• Hemoglobin-haptoglobin complex is then taken by
the RES where the hemoglobin fraction is broken
into iron and bilirubin
Hemoglobinuria vs myoglobinuria:
• Peroxidase acitivity using dipstick or chemstrips –
urine specimen
• Increased or normal free haptoglobinuria will
indicate myoglobinuria or rhabdomyolysis
65. BETA-LIPOPROTEIN
Low-density lipoprotein which has a
characteristic sharp leading edge and a
feathery trailing edge
66. TRANSFERRIN
• Also known as siderophilin
• Major beta-globulin protein
• Normally at 200 to 400 mg/dL
• Transport ferric ions from iron stores of
the intracellular or mucosal ferritin to bone
marrow where the red blood cells
precursors and other cells have
transferrin receptor on their surfaces
• Measured in terms of iron-binding
capacity – seen elevated in anemia
67. COMPLEMENT
• Travels with beta-globulins during the
electrophoresis
• C3 is decreased in autoimmune diseases
68. FIBRINOGEN
• Most abundant of the coagulation factors
• Elevation seen in pregnancies and the
use of birth control pills
• Decreased during the activation of
coagulation factors
• Migrates between beta and gamma
fractions
• Measured by Parfentjev method which
uses ammonium sulfate and sodium
chloride
69. MINOR PROTEINS
• Ceruloplasmin – Wilson‟s disease
(hepatolenticular degeneration)
• Gc-globulin – binds with vit D
• Hemopexin – prevent excretion of heme
and iron
• Alpha1-acid glycoprotein – increased
during pregnancy
• C-reactive protein – seen in tissue
necrosis; most sensitive acute phase
reactant located at chromosome 1