Protein structures by anivjeh
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tertiary and quaternary structures of protein molecules how long chain of amino acids (polypeptide) gets converted in to protein molecules
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C-A&P 05 Structural organization of proteins
This document summarizes the structural organization of proteins from primary to quaternary structure. It discusses that proteins have a unique amino acid sequence specified by genes which form the primary structure. The primary structure is stabilized by peptide bonds. Secondary structure involves folding into shapes like alpha helices and beta sheets held by hydrogen bonds. Tertiary structure involves the 3D shaping of the entire polypeptide chain through various interactions. Quaternary structure involves multiple polypeptide subunits combining to form a functional protein. Overall the document provides an overview of the hierarchical structural organization of proteins from sequence to final 3D shape.
Protein structure
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
Lecture 2 3 protein chemistry
Proteins are composed of amino acids linked by peptide bonds. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structures form based on hydrogen bonding patterns between amino acids. The two main secondary structures are the alpha helix, where amino acids coil into a helical shape, and the beta sheet, where amino acids align into beta strands connected by hydrogen bonds.
Main lecture for lipids
1. The document discusses different types of lipids including fatty acids, triglycerides, phospholipids, and steroids.
2. It explains the structures and properties of saturated and unsaturated fatty acids. Triglycerides are formed from glycerol and three fatty acids and are a major form of fat storage.
3. Phospholipids are a major component of cell membranes and contain a phosphate group. Cholesterol is an important sterol that is a component of cell membranes and precursor for other substances.
fatty acid synthesis.ppt
Fatty acid synthesis occurs in the cytosol and produces palmitic acid (C16:0). It involves the repeated condensation of acetyl-CoA units (derived from acetyl-CoA or malonyl-CoA) into a growing fatty acid chain on the acyl carrier protein. This is done through a cycle of condensation, reduction, dehydration, and reduction using NADPH as the reducing agent. The multi-enzyme fatty acid synthase complex contains seven enzymatic activities and adds two carbons with each cycle until palmitic acid is produced. Palmitic acid can then be further modified through elongation or desaturation to produce other fatty acids.
Lipid chemistry
This document outlines the key topics in lipid biochemistry. It begins by defining lipids as a heterogeneous group of organic compounds that are insoluble in water and can be extracted by nonpolar solvents. The document then discusses the structure and functions of the main types of lipids - fatty acids, triglycerides, phospholipids, and sterols. Important functions of lipids include energy storage, insulation, cell membrane structure, and as precursors to hormone-like molecules. An overview is also provided of lipid classification and the biochemical roles and importance of studying lipids.
PROTEINS
Proteins have a variety of important functions in living organisms. They are made up of chains of amino acids that join together to form complex structures ranging from simple primary to advanced quaternary structures which determine their specific roles. Globular proteins have spherical shapes defined by their amino acid sequences which allow metabolic functions like enzymatic reactions, while changes in structure through denaturation disrupt protein functioning.
Proteins
Proteins are made up of amino acids linked together by peptide bonds. The specific sequence and 3D structure of a protein determines its function. There are four levels of protein structure: primary structure is the amino acid sequence; secondary structure includes alpha helices and beta sheets from hydrogen bonding; tertiary structure is the overall folded shape from various weak interactions; and quaternary structure involves multiple protein subunits interacting.
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C-A&P 05 Structural organization of proteins
This document summarizes the structural organization of proteins from primary to quaternary structure. It discusses that proteins have a unique amino acid sequence specified by genes which form the primary structure. The primary structure is stabilized by peptide bonds. Secondary structure involves folding into shapes like alpha helices and beta sheets held by hydrogen bonds. Tertiary structure involves the 3D shaping of the entire polypeptide chain through various interactions. Quaternary structure involves multiple polypeptide subunits combining to form a functional protein. Overall the document provides an overview of the hierarchical structural organization of proteins from sequence to final 3D shape.
Protein structure
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
Lecture 2 3 protein chemistry
Proteins are composed of amino acids linked by peptide bonds. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structures form based on hydrogen bonding patterns between amino acids. The two main secondary structures are the alpha helix, where amino acids coil into a helical shape, and the beta sheet, where amino acids align into beta strands connected by hydrogen bonds.
Main lecture for lipids
1. The document discusses different types of lipids including fatty acids, triglycerides, phospholipids, and steroids.
2. It explains the structures and properties of saturated and unsaturated fatty acids. Triglycerides are formed from glycerol and three fatty acids and are a major form of fat storage.
3. Phospholipids are a major component of cell membranes and contain a phosphate group. Cholesterol is an important sterol that is a component of cell membranes and precursor for other substances.
fatty acid synthesis.ppt
Fatty acid synthesis occurs in the cytosol and produces palmitic acid (C16:0). It involves the repeated condensation of acetyl-CoA units (derived from acetyl-CoA or malonyl-CoA) into a growing fatty acid chain on the acyl carrier protein. This is done through a cycle of condensation, reduction, dehydration, and reduction using NADPH as the reducing agent. The multi-enzyme fatty acid synthase complex contains seven enzymatic activities and adds two carbons with each cycle until palmitic acid is produced. Palmitic acid can then be further modified through elongation or desaturation to produce other fatty acids.
Lipid chemistry
This document outlines the key topics in lipid biochemistry. It begins by defining lipids as a heterogeneous group of organic compounds that are insoluble in water and can be extracted by nonpolar solvents. The document then discusses the structure and functions of the main types of lipids - fatty acids, triglycerides, phospholipids, and sterols. Important functions of lipids include energy storage, insulation, cell membrane structure, and as precursors to hormone-like molecules. An overview is also provided of lipid classification and the biochemical roles and importance of studying lipids.
PROTEINS
Proteins have a variety of important functions in living organisms. They are made up of chains of amino acids that join together to form complex structures ranging from simple primary to advanced quaternary structures which determine their specific roles. Globular proteins have spherical shapes defined by their amino acid sequences which allow metabolic functions like enzymatic reactions, while changes in structure through denaturation disrupt protein functioning.
Proteins
Proteins are made up of amino acids linked together by peptide bonds. The specific sequence and 3D structure of a protein determines its function. There are four levels of protein structure: primary structure is the amino acid sequence; secondary structure includes alpha helices and beta sheets from hydrogen bonding; tertiary structure is the overall folded shape from various weak interactions; and quaternary structure involves multiple protein subunits interacting.
Protein folding
The document discusses protein folding, which is the process by which proteins achieve their functional three-dimensional structure from their linear amino acid sequence. It describes the different levels of protein structure, including primary, secondary, tertiary, and quaternary structure. The folding process depends on factors like temperature, pH, and molecular chaperones, which assist in protein folding. Proper folding is required for proteins to carry out their functions in the cell.
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Nucleic acids are made up of monomeric units called nucleotides. Nucleotides serve important biochemical functions as components of coenzymes involved in transferring phosphoryl, sugar, lipid groups. They also function as second messengers like cAMP and cGMP. Synthetic nucleotides containing halogens or additional nitrogen are used in chemotherapy and immunosuppression. Purines and pyrimidines are heterocyclic nitrogen-containing compounds that form the bases of nucleic acids. Nucleosides are derivatives of bases linked to a sugar, while nucleotides contain a phosphoryl group attached to the sugar. RNA and DNA are made up of ribonucleotides and deoxyribonucleotides formed through a series of phosphorylation and conversion reactions in
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The slides explain the structures of proteins, the bond stabilizing the structure of amino acids, the different types of protein structures, the applied aspects and the newer advances in the protein structure.
Protein
1. Protein is made up of amino acids that are linked together through peptide bonds to form polypeptide chains. The sequence and structure of these chains determines the protein's function.
2. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the sequence of amino acids. Secondary structures include alpha helices and beta sheets. Tertiary structure involves folding into a 3D shape. Quaternary involves multiple protein subunits.
3. Examples of important proteins and their structures include hemoglobin, which has a quaternary structure to transport oxygen in red blood cells, and collagen which has a triple helix structure that provides structure and connective
Protein Powerpoint
The document discusses the structure and formation of proteins. It explains that amino acids join through condensation reactions to form peptide bonds, releasing a water molecule. Multiple peptide bonds form polypeptide chains of varying lengths that fold into unique 3D shapes to serve as functional proteins, such as structural, storage, transport, hormonal, receptor, contractile, defensive, and enzymatic proteins. Common food sources of protein are also mentioned.
Protein structure
Proteins are composed of amino acids bonded together in chains called polypeptides. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the sequence of amino acids in the polypeptide chain. The secondary structure describes local folding patterns like alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure refers to the overall 3D shape formed by interactions between amino acids distant in the chain. Quaternary structure involves the interaction of multiple polypeptide chains. Changes in protein structure can alter its function.
Lipds
Lipids are composed of carbon, hydrogen, and oxygen. The three main classes of lipids are neutral fats, phospholipids, and steroids. Neutral fats serve as long-term energy stores. Phospholipids are structural components of cell membranes and regulate materials passing in and out of cells. Steroids include hormones and cholesterol, which provide stability to cell membranes.
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El documento describe las diferentes estructuras de las proteínas, incluyendo la estructura primaria que es la secuencia de aminoácidos, la estructura secundaria que incluye hélices alfa y láminas beta, la estructura terciaria que es el plegamiento tridimensional de la cadena polipeptídica, y en algunas proteínas la estructura cuaternaria que implica la asociación de múltiples cadenas polipeptídicas. También describe los diferentes tipos de interacciones como puentes de hidrógeno y disulfuro que
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Classification of amino acids
This document discusses the classification of amino acids. It summarizes that amino acids can be classified into different categories based on their R-group structure, polarity, nutritional requirements, and catabolism. The key classifications covered include non-polar vs polar amino acids, essential vs non-essential amino acids based on nutritional needs, and glucogenic, ketogenic, or mixed amino acids based on their metabolic fates. The document also provides examples of amino acids that fall into each of these different classification groups.
Lipids Ppt.
1. LIPIDS.
2. PROPERTIES OF LIPIDS.
3. FATTY ACIDS.
4. USES AND CLASSIFICATION OF FATTY ACIDS.
5. STRUCTURE AND CLASSIFICATION OF LIPIDS.
PHOSPHOLIPIDS: A class of lipid that is a key component of all cell membranes, as they can form lipid biomarkers. Composition: It is composed of phospholipids. i. Glycerol: one molecule ii. Fatty acids: Two molecules. iii. Phosphoric acid: one molecule. When a nitrogen-containing phospholipid group is attached to the end of the phospholipid, it is called phosphatidylcholine. Phospholipids consist of two parts i) Chapter: The head is polar in nature, soluble in water (hydrophilic). n) Tails: Nature has a non-polar tail, insoluble in water (hydrophobic).
Washes: Wax lipids are derived. Wax is a fatty acid ester and chronic alcohol: The wax is composed of i) a long-chain fatty acid ... one molecules ii) long-chain alcohol with one hydroxyl group (-OH), i.e. Cylinder wax is hydrophobic in nature. They have a high melting point, solid at room temperature. it gives stability and declines. On the surfaces of parts of plants, e.g. The leaves and fruits produce a waterproof layer, reducing the rate of perspiration. Wax is also a layer of wax that covers the bodies of animals, e.g., slime, insects, etc.
STEROIDS: Steroids fall under the lipid categories: Steroids are derived from lipid composition: proper arrangement of 3 cyclohexyl rings and 1 cyclopentane ring, a total of 17 carbon atoms in four carbon rings. Steroids do not contain alcohol and fatty acids.
Steroids Examples of steroids: i) Cholesterol: an important factor in animal cells. The precursor of all hormonal molecules such as aldosterone, sex hormone, and vitamin D ii) Aldosterone helps regulate Na+ions in the blood iii) Sex hormones e.g. testosterone, progesterone, and estrogens help to preserve the characteristics of males and females.
TERPENOIDES: It contains a very different class of organic compounds. Terpenoids are lipid derivatives, soluble in fat and soluble in water. Don't use molecule acids like fats. Composite units which they call isoprenoid or isoprenes. Isoprene unit: Hydrocarbon containing five carbon atoms with a branched-chain structure. Isoprene units bind to each other through the condensation process resulting in different types of compounds, e.g. Carotenoids, terpenes, and rubbers, etc.
CAROTENOIDS: Carotenoids are yellow, orange, red, or brown in plants. There are two kinds: i) Carotene: ii) Xanthophylla, i) Carotene: Orange is the genus of carotene, with red color, beta carotene. carrot & rice. Breakdown of beta-carotene leaves two molecules of vitamin A in the human body. n) Xanthophyllus: the auxiliary yellow color found in plants.
6 STORAGE LIPIDS.
7. USES OF LIPIDS.
# ALL ABOUT LIPIDS BY AUTHENTIC BOOKS.
Cl-05 : Steorids
Steroids are organic compounds composed of four fused carbon rings. Cholesterol is a steroid produced by the liver and consumed through meat and dairy. It contains one hydroxyl group and has an eight carbon side chain. Cholesterol is a component of cell membranes and is involved in the synthesis of bile acids, steroid hormones, and vitamin D. High cholesterol can lead to atherosclerosis and cardiovascular disease. Lifestyle changes like diet and exercise as well as statin drugs can help control cholesterol levels.
class-3 Derived lipids (steorids).pptx
1) Derived lipids are lipids obtained after hydrolysis of simple and complex lipids that possess characteristics of lipids, such as fatty acids and steroids.
2) Respiratory distress syndrome is caused by a deficiency of lecithin. The composition of lung surfactant includes dipalmitoyl lecithin, phosphatidyl glycerol, and surfactant proteins A, B, and C.
3) Fatty liver disease is characterized by too much fat in the liver and is caused by obesity, diabetes, and excessive alcohol consumption. Symptoms include fatigue, weight loss, and abdominal pain. Lipotropic factors like choline and methionine prevent fatty liver by reducing fat deposition
Proteins
Proteins have many important functions in the body including structure, catalysis, movement, transport, hormones, protection, storage, and regulation. They are composed of amino acids that are linked together through peptide bonds to form polypeptide chains or folded structures. The structure of proteins includes primary, secondary, tertiary, and sometimes quaternary levels that determine the protein's shape and function. Denaturation can disrupt a protein's structure through physical or chemical means.
Proteins
Proteins are composed of chains of amino acids and have four levels of structure: primary, secondary, tertiary, and quaternary. They perform many critical functions in the body as enzymes, hormones, antibodies, and structural components. Proteins can be classified based on their shape as globular or fibrous proteins, and based on their structural complexity as simple, conjugated, or derived proteins. They carry out roles in structures, functions, regulations, and protections in cells and tissues throughout the body.
Chemistry of amino acids&proteins
- Amino acids are the building blocks of proteins. They contain an amino group, a carboxyl group, an alpha carbon and different side chains attached to the alpha carbon.
- At physiological pH, amino acids exist as zwitterions with both positive and negative charges. There are 20 common amino acids that make up proteins. The order and structure of amino acids determines the structure and function of proteins.
- Amino acids can be classified based on their structure, side chains, nutritional requirements and metabolic fate. Many amino acids are essential and must be obtained through diet. Amino acids play important roles in human health and disease.
Proteins Structure
Proteins are the most abundant organic molecules in living systems, making up about 50% of cellular dry weight. They occur throughout the cell and form the basic structure and functions of life. All proteins are polymers of amino acids. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids joined by peptide bonds. Secondary structure involves hydrogen bonding that causes regions of the polypeptide chain to fold into alpha helices or beta sheets. Tertiary structure describes the three-dimensional shape that proteins fold into. Quaternary structure refers to complexes of multiple polypeptide subunits.
Protein and protein Dystrophin
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.
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Chemistry, classification & properties of carbohydrates
General methods of carbohydrates
Absorption, digestion, metabolism of carbohydrates
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Nucleic acids are made up of monomeric units called nucleotides. Nucleotides serve important biochemical functions as components of coenzymes involved in transferring phosphoryl, sugar, lipid groups. They also function as second messengers like cAMP and cGMP. Synthetic nucleotides containing halogens or additional nitrogen are used in chemotherapy and immunosuppression. Purines and pyrimidines are heterocyclic nitrogen-containing compounds that form the bases of nucleic acids. Nucleosides are derivatives of bases linked to a sugar, while nucleotides contain a phosphoryl group attached to the sugar. RNA and DNA are made up of ribonucleotides and deoxyribonucleotides formed through a series of phosphorylation and conversion reactions in
Proetin Tertiary Structure
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e.g. Globular proteins & Fibrous Proteins
Learning Keys , Lehninger Chapter # 3 Amino Acids,Peptides and Proteins
These Learning key Points will help when you will study Text Book of Lehninger Principles Of Biochemistry .
Structure of protiens and the applied aspects
The slides explain the structures of proteins, the bond stabilizing the structure of amino acids, the different types of protein structures, the applied aspects and the newer advances in the protein structure.
Protein
1. Protein is made up of amino acids that are linked together through peptide bonds to form polypeptide chains. The sequence and structure of these chains determines the protein's function.
2. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the sequence of amino acids. Secondary structures include alpha helices and beta sheets. Tertiary structure involves folding into a 3D shape. Quaternary involves multiple protein subunits.
3. Examples of important proteins and their structures include hemoglobin, which has a quaternary structure to transport oxygen in red blood cells, and collagen which has a triple helix structure that provides structure and connective
Protein Powerpoint
The document discusses the structure and formation of proteins. It explains that amino acids join through condensation reactions to form peptide bonds, releasing a water molecule. Multiple peptide bonds form polypeptide chains of varying lengths that fold into unique 3D shapes to serve as functional proteins, such as structural, storage, transport, hormonal, receptor, contractile, defensive, and enzymatic proteins. Common food sources of protein are also mentioned.
Protein structure
Proteins are composed of amino acids bonded together in chains called polypeptides. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the sequence of amino acids in the polypeptide chain. The secondary structure describes local folding patterns like alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure refers to the overall 3D shape formed by interactions between amino acids distant in the chain. Quaternary structure involves the interaction of multiple polypeptide chains. Changes in protein structure can alter its function.
Lipds
Lipids are composed of carbon, hydrogen, and oxygen. The three main classes of lipids are neutral fats, phospholipids, and steroids. Neutral fats serve as long-term energy stores. Phospholipids are structural components of cell membranes and regulate materials passing in and out of cells. Steroids include hormones and cholesterol, which provide stability to cell membranes.
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El documento describe las diferentes estructuras de las proteínas, incluyendo la estructura primaria que es la secuencia de aminoácidos, la estructura secundaria que incluye hélices alfa y láminas beta, la estructura terciaria que es el plegamiento tridimensional de la cadena polipeptídica, y en algunas proteínas la estructura cuaternaria que implica la asociación de múltiples cadenas polipeptídicas. También describe los diferentes tipos de interacciones como puentes de hidrógeno y disulfuro que
Tema 5
El documento describe la estructura y función de los nucleótidos y ácidos nucleicos. Explica que los nucleótidos son la unidad básica de los ácidos nucleicos y están formados por una pentosa, fosfato y base nitrogenada. Los ácidos nucleicos principales son el ADN y el ARN. El ADN forma una doble hélice y contiene la información genética, mientras que el ARN participa en la síntesis de proteínas. La cromatina contiene el ADN empaquetado en el núcleo celular gracias a
Lipid bio chemistry
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كيمياء حيوية جامعة الملك سعود
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كيمياء جامعية
0503964728
محمد منير كيمياء
ابو يوسف
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Classification of amino acids
This document discusses the classification of amino acids. It summarizes that amino acids can be classified into different categories based on their R-group structure, polarity, nutritional requirements, and catabolism. The key classifications covered include non-polar vs polar amino acids, essential vs non-essential amino acids based on nutritional needs, and glucogenic, ketogenic, or mixed amino acids based on their metabolic fates. The document also provides examples of amino acids that fall into each of these different classification groups.
Lipids Ppt.
1. LIPIDS.
2. PROPERTIES OF LIPIDS.
3. FATTY ACIDS.
4. USES AND CLASSIFICATION OF FATTY ACIDS.
5. STRUCTURE AND CLASSIFICATION OF LIPIDS.
PHOSPHOLIPIDS: A class of lipid that is a key component of all cell membranes, as they can form lipid biomarkers. Composition: It is composed of phospholipids. i. Glycerol: one molecule ii. Fatty acids: Two molecules. iii. Phosphoric acid: one molecule. When a nitrogen-containing phospholipid group is attached to the end of the phospholipid, it is called phosphatidylcholine. Phospholipids consist of two parts i) Chapter: The head is polar in nature, soluble in water (hydrophilic). n) Tails: Nature has a non-polar tail, insoluble in water (hydrophobic).
Washes: Wax lipids are derived. Wax is a fatty acid ester and chronic alcohol: The wax is composed of i) a long-chain fatty acid ... one molecules ii) long-chain alcohol with one hydroxyl group (-OH), i.e. Cylinder wax is hydrophobic in nature. They have a high melting point, solid at room temperature. it gives stability and declines. On the surfaces of parts of plants, e.g. The leaves and fruits produce a waterproof layer, reducing the rate of perspiration. Wax is also a layer of wax that covers the bodies of animals, e.g., slime, insects, etc.
STEROIDS: Steroids fall under the lipid categories: Steroids are derived from lipid composition: proper arrangement of 3 cyclohexyl rings and 1 cyclopentane ring, a total of 17 carbon atoms in four carbon rings. Steroids do not contain alcohol and fatty acids.
Steroids Examples of steroids: i) Cholesterol: an important factor in animal cells. The precursor of all hormonal molecules such as aldosterone, sex hormone, and vitamin D ii) Aldosterone helps regulate Na+ions in the blood iii) Sex hormones e.g. testosterone, progesterone, and estrogens help to preserve the characteristics of males and females.
TERPENOIDES: It contains a very different class of organic compounds. Terpenoids are lipid derivatives, soluble in fat and soluble in water. Don't use molecule acids like fats. Composite units which they call isoprenoid or isoprenes. Isoprene unit: Hydrocarbon containing five carbon atoms with a branched-chain structure. Isoprene units bind to each other through the condensation process resulting in different types of compounds, e.g. Carotenoids, terpenes, and rubbers, etc.
CAROTENOIDS: Carotenoids are yellow, orange, red, or brown in plants. There are two kinds: i) Carotene: ii) Xanthophylla, i) Carotene: Orange is the genus of carotene, with red color, beta carotene. carrot & rice. Breakdown of beta-carotene leaves two molecules of vitamin A in the human body. n) Xanthophyllus: the auxiliary yellow color found in plants.
6 STORAGE LIPIDS.
7. USES OF LIPIDS.
# ALL ABOUT LIPIDS BY AUTHENTIC BOOKS.
Cl-05 : Steorids
Steroids are organic compounds composed of four fused carbon rings. Cholesterol is a steroid produced by the liver and consumed through meat and dairy. It contains one hydroxyl group and has an eight carbon side chain. Cholesterol is a component of cell membranes and is involved in the synthesis of bile acids, steroid hormones, and vitamin D. High cholesterol can lead to atherosclerosis and cardiovascular disease. Lifestyle changes like diet and exercise as well as statin drugs can help control cholesterol levels.
class-3 Derived lipids (steorids).pptx
1) Derived lipids are lipids obtained after hydrolysis of simple and complex lipids that possess characteristics of lipids, such as fatty acids and steroids.
2) Respiratory distress syndrome is caused by a deficiency of lecithin. The composition of lung surfactant includes dipalmitoyl lecithin, phosphatidyl glycerol, and surfactant proteins A, B, and C.
3) Fatty liver disease is characterized by too much fat in the liver and is caused by obesity, diabetes, and excessive alcohol consumption. Symptoms include fatigue, weight loss, and abdominal pain. Lipotropic factors like choline and methionine prevent fatty liver by reducing fat deposition
Proteins
Proteins have many important functions in the body including structure, catalysis, movement, transport, hormones, protection, storage, and regulation. They are composed of amino acids that are linked together through peptide bonds to form polypeptide chains or folded structures. The structure of proteins includes primary, secondary, tertiary, and sometimes quaternary levels that determine the protein's shape and function. Denaturation can disrupt a protein's structure through physical or chemical means.
Proteins
Proteins are composed of chains of amino acids and have four levels of structure: primary, secondary, tertiary, and quaternary. They perform many critical functions in the body as enzymes, hormones, antibodies, and structural components. Proteins can be classified based on their shape as globular or fibrous proteins, and based on their structural complexity as simple, conjugated, or derived proteins. They carry out roles in structures, functions, regulations, and protections in cells and tissues throughout the body.
Chemistry of amino acids&proteins
- Amino acids are the building blocks of proteins. They contain an amino group, a carboxyl group, an alpha carbon and different side chains attached to the alpha carbon.
- At physiological pH, amino acids exist as zwitterions with both positive and negative charges. There are 20 common amino acids that make up proteins. The order and structure of amino acids determines the structure and function of proteins.
- Amino acids can be classified based on their structure, side chains, nutritional requirements and metabolic fate. Many amino acids are essential and must be obtained through diet. Amino acids play important roles in human health and disease.
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Similar to Protein structures by anivjeh
Proteins Structure
Proteins are the most abundant organic molecules in living systems, making up about 50% of cellular dry weight. They occur throughout the cell and form the basic structure and functions of life. All proteins are polymers of amino acids. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids joined by peptide bonds. Secondary structure involves hydrogen bonding that causes regions of the polypeptide chain to fold into alpha helices or beta sheets. Tertiary structure describes the three-dimensional shape that proteins fold into. Quaternary structure refers to complexes of multiple polypeptide subunits.
Protein and protein Dystrophin
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.
Protein Chemistry and Functions
This document provides information on the structure and properties of proteins. It discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets. Tertiary structure involves the folding of the polypeptide chain. Quaternary structure involves the assembly of multiple polypeptide subunits. Proteins are classified by function, structure, composition, and nutritional value. Proteins play many important roles in the human body and are used in various applications.
Protein structure
Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets formed by hydrogen bonding of the polypeptide chain. Tertiary structure refers to the overall three-dimensional shape that results from interactions between amino acid side chains. Quaternary structure involves interactions between multiple protein subunits.
Proteins.pdf
Proteins are polypeptide structures made up of one or more extended chains of residues from the amino acid. They provide a wide range of organism tasks, including as DNA replication, molecule transport, metabolic process catalysis, and cell structural support.
The albumins seen in vast quantities in egg whites typically have a distinct 3D structure as a result of bonds that form between the protein’s various amino acids. These bonds are broken by heating, exposing the hydrophobic (water-hating) amino acids that are typically maintained on the inside of the protein 1, 1 comma, 2 end superscript, 2, start superscript. In an effort to escape the water that surrounds them in the egg white, the hydrophobic amino acids will bind to one another, creating a protein network that gives the egg white structure and makes it white and opaque. Ta-da! Protein denaturation, thank you for another wonderful breakfast
Pengetahuan struktur, bentuk dan sintesa protein
The document discusses the four levels of protein structure: primary, secondary, tertiary, and quaternary. It explains that proteins are made of amino acids that are linked together via peptide bonds. The order and sequence of amino acids determines the primary structure. Hydrogen bonding leads to the formation of regular structures like alpha helices and beta sheets, which make up the secondary structure. Tertiary structure refers to the overall three-dimensional shape of the protein, which is stabilized by interactions between amino acid side chains. Some proteins have quaternary structure consisting of multiple polypeptide subunits.
Protein metabolism and nitrogen fixation and metabolism
- The document discusses protein metabolism and nitrogen fixation. It covers the classification of proteins based on their structure, composition, and functions. There are four levels of protein structure - primary, secondary, tertiary, and quaternary.
- The primary structure is the linear sequence of amino acids. The secondary structure involves folding into alpha helices or beta sheets via hydrogen bonding. Tertiary structure describes the overall 3D shape formed by interactions between amino acid R groups. Quaternary structure applies to proteins with multiple polypeptide chains that combine to form complexes.
- Proteins are classified as globular, fibrous, or intermediate based on their shape. They can also be simple or conjugated based on composition
Lec 2 level 3-de(chemistry of proteins)
Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure is the three-dimensional folding determined by interactions between secondary structures. Quaternary structure involves interactions between multiple polypeptide chains. Proteins can also be classified based on shape, function, and composition. Denaturation disrupts non-covalent bonds leading to loss of native structure and biological function.
BCH 803 Lecture.pptx
Proteins perform important functions like binding, catalysis, and acting as structural elements. There is a linear relationship between a gene's DNA sequence and the amino acid sequence of its encoded protein. Proteins have several levels of structure including primary, secondary, tertiary, and quaternary. The secondary structure includes alpha helices and beta sheets formed via hydrogen bonds between backbone peptide groups. Tertiary structure involves folding of these secondary elements into compact 3D structures stabilized by various interactions. Quaternary structure refers to complexes of multiple polypeptide chains held together by intermolecular forces.
Amino Acids and Protein
Study Material for B.Sc. Students
Primary, secondary, tertiary, quaternary structures of protein, motiffs and domains, subunits
AS Biology - Proteins
Proteins are made up of amino acid monomers that join together via condensation reactions to form polypeptide chains. A protein's primary structure is the sequence of its amino acids, which determines its higher order structures including secondary, tertiary, and possibly quaternary structures. These structures ultimately define a protein's specific 3D shape and functional role in the body, such as structural support, movement, or cellular communication.
Protein Sequence and Structure Data.pptx
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.
Protein structural organisation
Proteins play key roles in living systems through catalysis, transport, and information transfer. They have a hierarchical structure including primary, secondary, tertiary, and quaternary levels. The primary structure is the amino acid sequence, and higher levels of organization are determined by the primary structure. Protein folding and interactions between residues determine the final 3D tertiary and quaternary structures, which are critical for protein function. Misfolded proteins can cause diseases.
Quaternary structure of protein
Quaternary structure refers to the arrangement of multiple protein subunits into a single protein complex. Hemoglobin is a common example that is made of two alpha and two beta subunits. The subunits interact through hydrophobic interactions, hydrogen bonding, and other bonds. Globular proteins tend to have quaternary structure that clusters the subunits into a spherical shape, while fibrous proteins form long coils or sheets through interactions between subunits. Quaternary structure allows proteins to take on specialized functions beyond what individual subunits could achieve alone.
levels of protein structure , Domains ,motifs & Folds in protein structure
Protein structure is hierarchical, with four levels: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets formed by hydrogen bonding between amino acids in the sequence. Tertiary structure involves folding of the entire chain into a compact 3D structure. Quaternary structure involves the assembly of protein subunits. Other structural features include domains, which are independently folded and functional regions, motifs like loops and barrels formed by secondary structure elements, and folds defined by the arrangement of alpha helices and beta sheets. Understanding protein structure is important for studying protein function and for developing drugs.
Protein structure
Proteins are polymers made up of amino acid chains that form specific structures. There are four levels of protein structure:
1. Primary structure is the amino acid sequence.
2. Secondary structures include alpha helices and beta sheets formed by hydrogen bonds between amino acids.
3. Tertiary structure is the three dimensional folding of secondary structures.
4. Quaternary structure occurs in proteins made of multiple polypeptide chains that aggregate. The document discusses these levels of structure in detail, focusing on alpha helices and beta sheets as common secondary structures stabilized by hydrogen bonding.
Protein & amino acid (ulivina pratini)
This document discusses amino acids and proteins. It begins by defining proteins as polymers of amino acids and describing the basic structure of amino acids. It then covers the different configurations of amino acids, their properties in aqueous solutions, and classifications. The document also discusses the structures of peptides and proteins at the primary, secondary, tertiary, and quaternary levels. It describes the digestion and metabolism of amino acids as well as the urea cycle. Finally, it provides an overview of protein biosynthesis, including the roles of DNA, mRNA, tRNA, and ribosomes.
Lec 2 level 3-nu(structure of protein)
Proteins have four levels of structural organization: primary, secondary, tertiary, and quaternary. The primary structure refers to the linear sequence of amino acids in the polypeptide chain. Secondary structure involves local folding patterns like alpha helices and beta sheets. Tertiary structure describes the overall 3D shape of a single polypeptide chain. Quaternary structure is the 3D structure formed by the assembly of multiple polypeptide subunits. The structures at each level are stabilized by interactions between the R groups of amino acids in the chain.
Proteins & amino acids (ulivina pratini)
This document discusses amino acids and proteins. It begins by defining proteins as being formed from amino acids, which are the monomers or building blocks of proteins. The document then covers the structure of amino acids, including their general formula and configurations. It also discusses the properties of amino acids in aqueous solutions and their classification as essential or non-essential. The document goes on to explain how amino acids can bond together to form peptides and polypeptides, and the levels of protein structure from primary to quaternary. It concludes with sections on the metabolism of proteins and amino acids in the body.
Similar to Protein structures by anivjeh (20)
Protein metabolism and nitrogen fixation and metabolism
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Protein structures by anivjeh
- 2. Protein structures Proteins are highly complex organic nitrogenous macromolecule made up from carbon hydrogen oxygen & nitrogen Along with these amino acids also contains substances such as S, P, Co, Fe, Zn are also associated with proteins Proteins are made up from 20 amino acids Long chain of amino acid is called polypeptide 2 amino acids are linked together by means of peptide bond
- 3. Pauling & corey (1951) are the scientist who reported on protein structures Protein structure may varies from simple to complex to further complexity On complexity they are classify as: Primary Secondary Tertiary Quaternary
- 4. Primary structure These are simplest proteins having plain linear chain of amino acids They have 2 terminals one terminal is known as carboxyl end (C-terminal) and another terminal is known as amino end (N- terminal)
- 5. Secondary structure Folding of the linear poly peptide chain in to a specific coil represents the secondary structure The bonds can occur in same peptide chain &either between different polypeptide chain On complexity there are two different types of secondary structures Alpha helices Beta pleated sheets
- 6. Alpha helix : the polypeptide backbone tightly wound around an imaginary axis drawn longitudinally through the middle of helix Beta pleated sheets : the back bone of polypeptide chain is extend into zigzag rather than helical structures The zigzag polypeptide can arrange side by side to form structure resembling a series of pleats
- 7. Hydrogen bonding : it is mainly an electrostatic interaction between a weakly acidic donor (carboxyl group)& weakly basic acceptor (amino group)
- 8. Disulfide bond : It is formed by oxidation of the thiol or sulfhydryl ( -SH group) of 2 cysteine residues to yield a molecule of cystine Bond of shortest range it is also known as sulphur bridge
- 9. Ionic Bond : ions of similar charges repel with each other and that of dissimilar charges attract each other This is also called as Electrostatic bond
- 10. Hydrophobic Bond : many amino acid contains non polar side chains , which are hydrophobic in nature these hydrophobic sides of different groups tend to associate themselves to remain away from water It is also know as Non polar Bond or van der waals interactions
- 11. Tertiary structure It is a folding of secondary structural elements and it also specifies the positions of each atom in the protein molecule The protein structure can be determined through X-ray Crystallography or Nuclear magnetic resonance (NMR) Large polypeptide containing more than 200 a.a folds in to cluster are known as Domain They are classify in to Fibrous proteins & Globular proteins
- 12. Fibrous proteins polypeptide chains arrange in long strands or sheets They contain single type of secondary structure They are insoluble in water They provide structural support , shape, flexibility, strength & external protection Eg: alpha keratin, collagen & silk fibroin
- 13. Globular proteins Polypeptide chains folded into spherical or globular shape Poly peptide with few hundred a.a residues often fold into two or more stable , globular units called as domains They carried out wide array of biological functions such as enzymes, motor proteins, transport proteins, regulatory proteins, immunoglobulins.
- 14. Folding patterns in proteins
- 15. Quaternary structures The quaternary structure involves the Non-Covalent association of one or more peptide chains There are two types of quaternary structures Multimer : it is composed of non identical subunits They are also called as oligomer Oligomers may have either rotational or helical symmetry Protomer : it is composed of same structural subunits Eg: hemoglobin, nucleosomes and microtubules.
- 18. Refrences Lehninger principles of biochemistry by David L. Nelson & Michael M.Cox Plant physiology by S.Mukherji & A K Ghosh
- 19. Thanking you