Proteins
•Download as PPT, PDF•
0 likes•541 views
Proteins are essential biomolecules that are derived from the Greek word "protos" meaning "I occupy". They play important roles in forming living cells, carrying genetic information as nucleoproteins, catalyzing biochemical reactions as enzymes, making up viruses, providing energy, and performing specialized functions such as oxygen transport and hormone activity. Proteins can be classified based on their physical and chemical properties, functions, and structures into categories like simple proteins including albumin, globulin, and globin; compound proteins; and derived proteins.
Report
Share
Report
Share
Recommended
PROTEINS
includes structure of proteins, types of proteins ,properties of proteins ,can use as a quick resource for presenting a seminar
Biomolecules carbohydrate
Biomolecules are organic and inorganic chemicals that occur in living organisms. They include carbohydrates, proteins, lipids, nucleic acids, and other molecules. Biomolecules can be classified as either micromolecules, which are small and soluble, or macromolecules, which are large polymers formed from micromolecules. The four major types of biomolecules - carbohydrates, nucleic acids, lipids, and proteins - differ in their composition and functions, which include energy storage, heredity, structure, and catalysis of biological processes.
Proteoglycans sb
This document defines and describes several types of biomolecules:
- Proteoglycans are macromolecules found in the extracellular matrix containing glycosaminoglycan chains covalently bonded to proteins. They form connective tissue and regulate molecule movement.
- Glycoproteins contain oligosaccharide chains bonded to proteins and are found on cell surfaces and in extracellular matrices. They facilitate protein recognition and binding.
- Lipopolysaccharides are toxic components of gram-negative bacterial outer membranes that trigger immune responses.
- Lipoproteins transport lipids through the bloodstream with a lipid core and phospholipid shell. Apolipoproteins are structural and functional protein components.
- Proteolipids contain co
Classification of Protein by different mode.
• Description: In this video the viewers will come to know about different mode of classification of proteins. Proteins are classified based on their Solubility and composition, Function, Shape & size.
Portion explained:
Classification based on solubility and composition
Simple proteins
1. Albumins
2. Globulins
3. Prolamins
4. Glutelins
5. Histones
6. Protamines
7. Albuminoids
ii. Conjugated or compound proteins
1. Nucleoproteins
2. Mucoproteins
3. Chromoproteins
4. Lipoproteins
5. Metalloproteins
6. Phosphoproteins
B. Classification of proteins based on function
1. Catalytic proteins – Enzymes
2. Regulatory proteins – Hormones
3. Protective proteins – Antibodies
4. Storage proteins
5. Transport proteins
6. Toxic proteins
7. Structural proteins
8. Contractile proteins
9. Secretary proteins
10. Exotic proteins
C. Classification based on size and shape
Protein
Proteins are polymers of amino acids that perform a wide variety of essential functions in organisms. They are classified based on their function, chemical properties, nutritional content, and 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. Tertiary structure refers to the three-dimensional folding of the polypeptide chain. Quaternary structure involves the assembly of multiple protein subunits. Protein structure is stabilized by covalent bonds like peptide bonds as well as non-covalent interactions.
Proteins properties
Tertiary structure refers to the spatial arrangement of secondary structures in a protein. It is stabilized through hydrogen bonds, ionic interactions, hydrophobic interactions, and disulfide bonds. There are two main classifications of protein tertiary structure - globular proteins which have a spheroid shape with abundant secondary structures, and fibrous proteins which are rod-shaped with one predominant secondary structure like collagen. Quaternary structure refers to the structure formed when two or more protein subunits (polypeptide chains) combine through non-covalent interactions. Denaturation involves the unfolding of protein structures due to factors like heat, salts, pH, or mechanical action and is partially reversible. Coagulation follows denaturation and involves the irre
Structure, Chemical Properties, and Function of Proteins, Intracellular Traff...
Proteins are an important class of biological macromolecules which are the polymers of amino acids.
Lipoproteins , Lec 62.
The document discusses the metabolism of lipoproteins in the human body. It describes the main classes of lipoproteins - chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) - and their functions in transporting lipids around the body. Specifically, it notes that chylomicrons carry dietary lipids from the intestines to tissues, VLDL transports endogenous triglycerides from the liver to tissues, and changes to these lipoproteins during metabolism are facilitated by various apolipoproteins. The metabolism of lipoproteins is important as improper levels can contribute to atherosclerosis.
Recommended
PROTEINS
includes structure of proteins, types of proteins ,properties of proteins ,can use as a quick resource for presenting a seminar
Biomolecules carbohydrate
Biomolecules are organic and inorganic chemicals that occur in living organisms. They include carbohydrates, proteins, lipids, nucleic acids, and other molecules. Biomolecules can be classified as either micromolecules, which are small and soluble, or macromolecules, which are large polymers formed from micromolecules. The four major types of biomolecules - carbohydrates, nucleic acids, lipids, and proteins - differ in their composition and functions, which include energy storage, heredity, structure, and catalysis of biological processes.
Proteoglycans sb
This document defines and describes several types of biomolecules:
- Proteoglycans are macromolecules found in the extracellular matrix containing glycosaminoglycan chains covalently bonded to proteins. They form connective tissue and regulate molecule movement.
- Glycoproteins contain oligosaccharide chains bonded to proteins and are found on cell surfaces and in extracellular matrices. They facilitate protein recognition and binding.
- Lipopolysaccharides are toxic components of gram-negative bacterial outer membranes that trigger immune responses.
- Lipoproteins transport lipids through the bloodstream with a lipid core and phospholipid shell. Apolipoproteins are structural and functional protein components.
- Proteolipids contain co
Classification of Protein by different mode.
• Description: In this video the viewers will come to know about different mode of classification of proteins. Proteins are classified based on their Solubility and composition, Function, Shape & size.
Portion explained:
Classification based on solubility and composition
Simple proteins
1. Albumins
2. Globulins
3. Prolamins
4. Glutelins
5. Histones
6. Protamines
7. Albuminoids
ii. Conjugated or compound proteins
1. Nucleoproteins
2. Mucoproteins
3. Chromoproteins
4. Lipoproteins
5. Metalloproteins
6. Phosphoproteins
B. Classification of proteins based on function
1. Catalytic proteins – Enzymes
2. Regulatory proteins – Hormones
3. Protective proteins – Antibodies
4. Storage proteins
5. Transport proteins
6. Toxic proteins
7. Structural proteins
8. Contractile proteins
9. Secretary proteins
10. Exotic proteins
C. Classification based on size and shape
Protein
Proteins are polymers of amino acids that perform a wide variety of essential functions in organisms. They are classified based on their function, chemical properties, nutritional content, and 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. Tertiary structure refers to the three-dimensional folding of the polypeptide chain. Quaternary structure involves the assembly of multiple protein subunits. Protein structure is stabilized by covalent bonds like peptide bonds as well as non-covalent interactions.
Proteins properties
Tertiary structure refers to the spatial arrangement of secondary structures in a protein. It is stabilized through hydrogen bonds, ionic interactions, hydrophobic interactions, and disulfide bonds. There are two main classifications of protein tertiary structure - globular proteins which have a spheroid shape with abundant secondary structures, and fibrous proteins which are rod-shaped with one predominant secondary structure like collagen. Quaternary structure refers to the structure formed when two or more protein subunits (polypeptide chains) combine through non-covalent interactions. Denaturation involves the unfolding of protein structures due to factors like heat, salts, pH, or mechanical action and is partially reversible. Coagulation follows denaturation and involves the irre
Structure, Chemical Properties, and Function of Proteins, Intracellular Traff...
Proteins are an important class of biological macromolecules which are the polymers of amino acids.
Lipoproteins , Lec 62.
The document discusses the metabolism of lipoproteins in the human body. It describes the main classes of lipoproteins - chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) - and their functions in transporting lipids around the body. Specifically, it notes that chylomicrons carry dietary lipids from the intestines to tissues, VLDL transports endogenous triglycerides from the liver to tissues, and changes to these lipoproteins during metabolism are facilitated by various apolipoproteins. The metabolism of lipoproteins is important as improper levels can contribute to atherosclerosis.
Peptides and proteins
Sindh Biotechnologist Association has taken initiative for all young scientists, researchers, and students to have the platform to show their talent and interest in different activities.
Topic: Peptides and Proteins
Presented by Sana Aurangzeb
For video Lecture: https://www.youtube.com/watch?v=KSadkkoUDCo
Mewar institute of management biochem
This document discusses protein catabolism, which is the breakdown of proteins into amino acids and other simple compounds. It describes how proteins are broken down through digestion and by proteases within cells. The amino acids produced can be used to form new proteins, converted into different amino acids, or further broken down through amino acid catabolism pathways like the Krebs cycle to generate energy. Key aspects of protein catabolism include factors that determine the rate like pH and temperature, and how amino acids gained can be used for protein synthesis or completely degraded for energy release.
Chemistry of lipids phospholipids
- Phospholipids are amphipathic lipids that contain fatty acids, glycerol, and a phosphate group. They form bilayer structures in cell membranes.
- Examples include phosphatidylcholine (lecithin), sphingomyelin, phosphatidylethanolamine. They play important structural and functional roles in membranes.
- Phospholipids can form micelles and liposomes in aqueous solutions due to their amphipathic nature. Liposomes are used as carriers for drug delivery.
- Lung surfactants contain lecithin and help reduce surface tension in the lungs. Deficiencies can cause respiratory distress in infants.
Biochem
This document discusses the components of the extracellular matrix (ECM), focusing on glycosaminoglycans. It explains that glycosaminoglycans are large heteropolysaccharide chains that bind water to form a gel-like matrix. They associate with small amounts of protein to form proteoglycans. Glycosaminoglycans provide flexibility and structure to the ECM and influence movement through it. They bind with water and structural proteins like collagen and elastin to form the body's ground substance and ECM. Most glycosaminoglycans are found attached to core proteins to form proteoglycan monomers in a "bottle brush" structure.
Macromolecular structure and biological function of primary protiens
This document discusses primary proteins, their structure and functions. It begins with defining proteins as polymers of amino acids linked by peptide bonds. It then discusses the primary structure of proteins, which is the linear arrangement of amino acids. The key functions of proteins mentioned include acting as antibodies, enzymes, hormones, for transport, storage, as structural proteins, and contractile proteins. Some applications discussed are using proteins in coatings, food packaging, biotechnology, foods, microchips, and biomedical applications like hydrogels and targeted drug delivery.
Proteoglycan
Proteoglycans are proteins that are covalently linked to glycosaminoglycans. They play several important roles in the extracellular matrix and tissues. Proteoglycans interact with collagen and elastin in the extracellular matrix. They also attract water into tissues through their negatively charged sulfate groups, act as barriers to pathogens, and aid in the release and transport of hormones and enzymes. Common proteoglycans include hyaluronic acid, keratin sulfate, chondroitin sulfate, and heparin.
Globular and fibrous proteins
This document summarizes and provides examples of two main types of proteins: fibrous proteins and globular proteins. Fibrous proteins have little tertiary structure and form long fibers or sheets through cross-linkages of parallel polypeptide chains. They are usually insoluble and structural, such as keratin and collagen. Globular proteins have complex 3D structures that are folded into spherical shapes. They are usually soluble and play roles in metabolic reactions as enzymes and hemoglobin. Hemoglobin and collagen are provided as examples, with hemoglobin being globular and oxygen-carrying, while collagen is fibrous and structural in skin, bones and other tissues.
Information about Cell and it's structure and protein synthesis
It gives information about Cell how it is discovered and it's structure and also it includes information about protein synthesis, it's structure and their simple notes.
membrane models and biosynthesis
Membranes are formed by complex lipids that spontaneously self-assemble into a lipid bilayer structure. The lipid bilayer is composed of two lipid monolayers with hydrophilic head groups facing outwards and hydrophobic tails buried inside. Integral membrane proteins span the bilayer, while peripheral proteins are attached to either surface. Membranes compartmentalize cells and carry out important functions like selective transport and signal transduction.
Protein structure & function
Proteins have a variety of functions in cells including enzymes, structural components, transporters, motors, and signaling molecules. A protein's unique 3D shape, determined by its amino acid sequence, allows it to carry out its specific function. The polypeptide backbone forms secondary structures like alpha helices and beta sheets. Non-covalent interactions further guide protein folding into a stable tertiary structure. Quaternary structure involves interactions between multiple polypeptide chains. Post-translational modifications and ligand binding regulate protein activity.
Cholesterol
Steroids are a class of lipids found in eukaryotic cell membranes and rarely in some bacteria. Cholesterol is a type of steroid or modified steroid that is an essential structural component of animal cell membranes. It is required to maintain membrane integrity and fluidity. Cholesterol also serves as a precursor for the biosynthesis of steroid hormones, bile acids, and vitamin D. Within cells, cholesterol is converted to bile salts which help to emulsify and absorb dietary fats in the small intestine. Bile salts are then reabsorbed and recycled through enterohepatic circulation.
Protein Structure and Function
A short presentation about protein, its structure, function. Also includes integral membrane protein and its uses.
Membrane fusion
This document discusses membrane fusion, a process by which two lipid bilayers merge together. It begins by defining membrane fusion and the intermediary state of hemifusion. It then discusses the challenges of overcoming energy barriers during fusion and the role of fusion proteins in lowering these barriers. The document outlines the typical four step process for membrane fusion to occur. It also discusses specific examples of membrane fusion in viruses, mitochondria, cells, and synaptic vesicles. Key proteins involved in different fusion processes like SNAREs and viral fusion proteins are also mentioned.
Lecture 1
This document classifies enzymes into six main categories based on the reactions they catalyze: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. It then provides examples of subclasses within some of these categories and briefly describes two models of enzyme-substrate binding - the lock and key model and induced fit model.
1.5 proteins UEC Senior 1 Biology 独中高一生物
The document summarizes key concepts about protein structure and types of proteins. It contains the following key points:
1. Protein structure is organized into four levels: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence, secondary structure involves coiling and folding into shapes like alpha helices and beta sheets. Tertiary structure involves further compact folding, and quaternary structure involves multiple polypeptide chains combining.
2. Proteins can be simple, only containing amino acids, or conjugated, containing non-polypeptide groups. Simple proteins include fibrous (insoluble) and globular (soluble) types. Conjugated proteins include nucleopro
protien slideshare
Proteins are made up of amino acids and perform essential functions in the body. They have a primary structure consisting of a sequence of amino acids. The amino acids then form secondary structures like alpha helices and beta sheets. Tertiary structure occurs when the polypeptide chain folds upon itself, stabilized by various bonds. Quaternary structure involves multiple protein subunits. There are two main types of proteins - fibrous proteins which are insoluble and provide structure, and globular proteins which are soluble and perform roles like enzyme catalysis. Proteins are essential for growth, cell structure, biochemical reactions, transport, immune function and more.
Sphingolipids
Sphingolipids are a class of lipids that include sphingomyelin, glycosphingolipids, and ceramide. They serve important structural and signaling functions in the cell membrane and participate in processes like cell growth, differentiation, and apoptosis. Sphingolipids are synthesized through de novo pathways or through the breakdown of sphingomyelin. Their metabolites, including ceramide, sphingosine-1-phosphate, and gangliosides act as second messengers and influence pathways such as PI3K/Akt and JNK. Sphingolipids are also components of lipid rafts and caveolae, which regulate protein activity and cellular signaling. Imbalances in sph
Enzymes
Enzymes are biological catalysts that are usually proteins and help speed up complex chemical reactions in living organisms. They have highly specific three-dimensional structures that allow them to bind to substrates and lower the activation energy of reactions. Enzymatic activity can be affected by factors like temperature, pH, inhibitors, and activators. Enzymes play crucial roles like catalyzing metabolic reactions, producing energy in the form of ATP through electron transport, acting as molecular motors, and performing the catabolic and anabolic processes of breaking down and building up molecules.
Fibrous proteinss
The document discusses fibrous proteins and collagen. It provides details on:
1) Fibrous proteins are usually insoluble and found in skin, connective tissue, blood vessels and other structures. They have high alpha-helix or beta-sheet content and examples include collagen, elastin, keratin and fibroin.
2) Collagen is the most abundant fibrous protein, making up 25-35% of the body's protein. It provides structure and strength, and there are at least 19 types designated by Roman numerals.
3) Collagen has a characteristic amino acid sequence of glycine-X-Y where X is often proline and Y can be hydroxyproline or hydroxy
10 polysacch. _heteroglycosides__nucleic_acids
- Polysaccharides are biopolymers made of monosaccharide units linked by glycosidic bonds that can be classified as homopolysaccharides or heteropolysaccharides.
- Starch is a homopolysaccharide energy storage molecule in plants composed of amylose and highly branched amylopectin. Glycogen is the analogous molecule that serves as energy storage in animals.
- Cellulose is an important structural heteropolysaccharide in plants composed of linear chains of beta-glucose units and forms part of insoluble dietary fiber.
Proteins
This document discusses proteins and their structure. It begins by introducing proteins and their composition of amino acids linked into peptide chains. It then describes the 20 main amino acids and how they are classified. The four levels of protein structural organization - primary, secondary, tertiary, and quaternary structure - are outlined. Common secondary structures like the alpha helix and beta sheet are also defined. Specific proteins like hemoglobin and myoglobin are then examined in more detail, including their subunit composition and role in oxygen transport.
7 regulation of metabolism
This document discusses the mechanisms of hormone and neurotransmitter action in the body. It describes the different types of receptors, including membrane receptors and intracellular receptors. It also explains the various signal transduction pathways triggered by receptors, such as G protein-coupled receptors that activate adenylate cyclase or phospholipase C, receptors with intrinsic enzymatic activity like guanylate cyclase, and receptors with tyrosine kinase activity like the insulin receptor. The key second messengers produced by these pathways, like cAMP, Ca2+, cGMP, and phosphorylated proteins, are also outlined.
More Related Content
What's hot
Peptides and proteins
Sindh Biotechnologist Association has taken initiative for all young scientists, researchers, and students to have the platform to show their talent and interest in different activities.
Topic: Peptides and Proteins
Presented by Sana Aurangzeb
For video Lecture: https://www.youtube.com/watch?v=KSadkkoUDCo
Mewar institute of management biochem
This document discusses protein catabolism, which is the breakdown of proteins into amino acids and other simple compounds. It describes how proteins are broken down through digestion and by proteases within cells. The amino acids produced can be used to form new proteins, converted into different amino acids, or further broken down through amino acid catabolism pathways like the Krebs cycle to generate energy. Key aspects of protein catabolism include factors that determine the rate like pH and temperature, and how amino acids gained can be used for protein synthesis or completely degraded for energy release.
Chemistry of lipids phospholipids
- Phospholipids are amphipathic lipids that contain fatty acids, glycerol, and a phosphate group. They form bilayer structures in cell membranes.
- Examples include phosphatidylcholine (lecithin), sphingomyelin, phosphatidylethanolamine. They play important structural and functional roles in membranes.
- Phospholipids can form micelles and liposomes in aqueous solutions due to their amphipathic nature. Liposomes are used as carriers for drug delivery.
- Lung surfactants contain lecithin and help reduce surface tension in the lungs. Deficiencies can cause respiratory distress in infants.
Biochem
This document discusses the components of the extracellular matrix (ECM), focusing on glycosaminoglycans. It explains that glycosaminoglycans are large heteropolysaccharide chains that bind water to form a gel-like matrix. They associate with small amounts of protein to form proteoglycans. Glycosaminoglycans provide flexibility and structure to the ECM and influence movement through it. They bind with water and structural proteins like collagen and elastin to form the body's ground substance and ECM. Most glycosaminoglycans are found attached to core proteins to form proteoglycan monomers in a "bottle brush" structure.
Macromolecular structure and biological function of primary protiens
This document discusses primary proteins, their structure and functions. It begins with defining proteins as polymers of amino acids linked by peptide bonds. It then discusses the primary structure of proteins, which is the linear arrangement of amino acids. The key functions of proteins mentioned include acting as antibodies, enzymes, hormones, for transport, storage, as structural proteins, and contractile proteins. Some applications discussed are using proteins in coatings, food packaging, biotechnology, foods, microchips, and biomedical applications like hydrogels and targeted drug delivery.
Proteoglycan
Proteoglycans are proteins that are covalently linked to glycosaminoglycans. They play several important roles in the extracellular matrix and tissues. Proteoglycans interact with collagen and elastin in the extracellular matrix. They also attract water into tissues through their negatively charged sulfate groups, act as barriers to pathogens, and aid in the release and transport of hormones and enzymes. Common proteoglycans include hyaluronic acid, keratin sulfate, chondroitin sulfate, and heparin.
Globular and fibrous proteins
This document summarizes and provides examples of two main types of proteins: fibrous proteins and globular proteins. Fibrous proteins have little tertiary structure and form long fibers or sheets through cross-linkages of parallel polypeptide chains. They are usually insoluble and structural, such as keratin and collagen. Globular proteins have complex 3D structures that are folded into spherical shapes. They are usually soluble and play roles in metabolic reactions as enzymes and hemoglobin. Hemoglobin and collagen are provided as examples, with hemoglobin being globular and oxygen-carrying, while collagen is fibrous and structural in skin, bones and other tissues.
Information about Cell and it's structure and protein synthesis
It gives information about Cell how it is discovered and it's structure and also it includes information about protein synthesis, it's structure and their simple notes.
membrane models and biosynthesis
Membranes are formed by complex lipids that spontaneously self-assemble into a lipid bilayer structure. The lipid bilayer is composed of two lipid monolayers with hydrophilic head groups facing outwards and hydrophobic tails buried inside. Integral membrane proteins span the bilayer, while peripheral proteins are attached to either surface. Membranes compartmentalize cells and carry out important functions like selective transport and signal transduction.
Protein structure & function
Proteins have a variety of functions in cells including enzymes, structural components, transporters, motors, and signaling molecules. A protein's unique 3D shape, determined by its amino acid sequence, allows it to carry out its specific function. The polypeptide backbone forms secondary structures like alpha helices and beta sheets. Non-covalent interactions further guide protein folding into a stable tertiary structure. Quaternary structure involves interactions between multiple polypeptide chains. Post-translational modifications and ligand binding regulate protein activity.
Cholesterol
Steroids are a class of lipids found in eukaryotic cell membranes and rarely in some bacteria. Cholesterol is a type of steroid or modified steroid that is an essential structural component of animal cell membranes. It is required to maintain membrane integrity and fluidity. Cholesterol also serves as a precursor for the biosynthesis of steroid hormones, bile acids, and vitamin D. Within cells, cholesterol is converted to bile salts which help to emulsify and absorb dietary fats in the small intestine. Bile salts are then reabsorbed and recycled through enterohepatic circulation.
Protein Structure and Function
A short presentation about protein, its structure, function. Also includes integral membrane protein and its uses.
Membrane fusion
This document discusses membrane fusion, a process by which two lipid bilayers merge together. It begins by defining membrane fusion and the intermediary state of hemifusion. It then discusses the challenges of overcoming energy barriers during fusion and the role of fusion proteins in lowering these barriers. The document outlines the typical four step process for membrane fusion to occur. It also discusses specific examples of membrane fusion in viruses, mitochondria, cells, and synaptic vesicles. Key proteins involved in different fusion processes like SNAREs and viral fusion proteins are also mentioned.
Lecture 1
This document classifies enzymes into six main categories based on the reactions they catalyze: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. It then provides examples of subclasses within some of these categories and briefly describes two models of enzyme-substrate binding - the lock and key model and induced fit model.
1.5 proteins UEC Senior 1 Biology 独中高一生物
The document summarizes key concepts about protein structure and types of proteins. It contains the following key points:
1. Protein structure is organized into four levels: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence, secondary structure involves coiling and folding into shapes like alpha helices and beta sheets. Tertiary structure involves further compact folding, and quaternary structure involves multiple polypeptide chains combining.
2. Proteins can be simple, only containing amino acids, or conjugated, containing non-polypeptide groups. Simple proteins include fibrous (insoluble) and globular (soluble) types. Conjugated proteins include nucleopro
protien slideshare
Proteins are made up of amino acids and perform essential functions in the body. They have a primary structure consisting of a sequence of amino acids. The amino acids then form secondary structures like alpha helices and beta sheets. Tertiary structure occurs when the polypeptide chain folds upon itself, stabilized by various bonds. Quaternary structure involves multiple protein subunits. There are two main types of proteins - fibrous proteins which are insoluble and provide structure, and globular proteins which are soluble and perform roles like enzyme catalysis. Proteins are essential for growth, cell structure, biochemical reactions, transport, immune function and more.
Sphingolipids
Sphingolipids are a class of lipids that include sphingomyelin, glycosphingolipids, and ceramide. They serve important structural and signaling functions in the cell membrane and participate in processes like cell growth, differentiation, and apoptosis. Sphingolipids are synthesized through de novo pathways or through the breakdown of sphingomyelin. Their metabolites, including ceramide, sphingosine-1-phosphate, and gangliosides act as second messengers and influence pathways such as PI3K/Akt and JNK. Sphingolipids are also components of lipid rafts and caveolae, which regulate protein activity and cellular signaling. Imbalances in sph
Enzymes
Enzymes are biological catalysts that are usually proteins and help speed up complex chemical reactions in living organisms. They have highly specific three-dimensional structures that allow them to bind to substrates and lower the activation energy of reactions. Enzymatic activity can be affected by factors like temperature, pH, inhibitors, and activators. Enzymes play crucial roles like catalyzing metabolic reactions, producing energy in the form of ATP through electron transport, acting as molecular motors, and performing the catabolic and anabolic processes of breaking down and building up molecules.
Fibrous proteinss
The document discusses fibrous proteins and collagen. It provides details on:
1) Fibrous proteins are usually insoluble and found in skin, connective tissue, blood vessels and other structures. They have high alpha-helix or beta-sheet content and examples include collagen, elastin, keratin and fibroin.
2) Collagen is the most abundant fibrous protein, making up 25-35% of the body's protein. It provides structure and strength, and there are at least 19 types designated by Roman numerals.
3) Collagen has a characteristic amino acid sequence of glycine-X-Y where X is often proline and Y can be hydroxyproline or hydroxy
10 polysacch. _heteroglycosides__nucleic_acids
- Polysaccharides are biopolymers made of monosaccharide units linked by glycosidic bonds that can be classified as homopolysaccharides or heteropolysaccharides.
- Starch is a homopolysaccharide energy storage molecule in plants composed of amylose and highly branched amylopectin. Glycogen is the analogous molecule that serves as energy storage in animals.
- Cellulose is an important structural heteropolysaccharide in plants composed of linear chains of beta-glucose units and forms part of insoluble dietary fiber.
What's hot (20)
Macromolecular structure and biological function of primary protiens
Macromolecular structure and biological function of primary protiens
Information about Cell and it's structure and protein synthesis
Information about Cell and it's structure and protein synthesis
Viewers also liked
Proteins
This document discusses proteins and their structure. It begins by introducing proteins and their composition of amino acids linked into peptide chains. It then describes the 20 main amino acids and how they are classified. The four levels of protein structural organization - primary, secondary, tertiary, and quaternary structure - are outlined. Common secondary structures like the alpha helix and beta sheet are also defined. Specific proteins like hemoglobin and myoglobin are then examined in more detail, including their subunit composition and role in oxygen transport.
7 regulation of metabolism
This document discusses the mechanisms of hormone and neurotransmitter action in the body. It describes the different types of receptors, including membrane receptors and intracellular receptors. It also explains the various signal transduction pathways triggered by receptors, such as G protein-coupled receptors that activate adenylate cyclase or phospholipase C, receptors with intrinsic enzymatic activity like guanylate cyclase, and receptors with tyrosine kinase activity like the insulin receptor. The key second messengers produced by these pathways, like cAMP, Ca2+, cGMP, and phosphorylated proteins, are also outlined.
B.Sc. Biochem II Biomolecule I U 3.2 Classification of Protein & Denaturation
This document discusses the classification and denaturation of proteins. It describes how proteins can be classified based on their structure, biological function, shape and solubility, composition, and nutritional basis. The main types of proteins classified by function include enzymes, transport proteins, storage proteins, contractile/motile proteins, structural proteins, and regulatory proteins. The document also discusses how proteins can be denatured, or lose their tertiary structure, through the application of heat, acids, bases, alcohols, heavy metal salts, and other stresses. Denaturation disrupts the bonding interactions that give proteins their shape.
4.3 proteins
Proteins are made up of elements like carbon, hydrogen, oxygen, nitrogen, sulfur, and phosphorus. They are formed through condensation reactions between amino acids and can be broken down through hydrolysis. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids, secondary structure involves alpha helices and beta sheets, tertiary is the overall 3D shape, and quaternary involves combinations of tertiary structures. There are essential and non-essential amino acids, with essential ones not synthesized by the body.
Structure of organic compounds
Biochemistry is the study of chemical composition and reactions in living matter. It includes inorganic compounds like water and CO2, as well as organic compounds composed of carbon, hydrogen, and oxygen. Organic compounds are made of polymers of monomers like carbohydrates, lipids, proteins, and nucleic acids. These macromolecules are essential to life processes in cells and provide structure, energy storage, homeostasis, and genetic information.
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
Proteins are composed of amino acids and play many essential roles in the body. They have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence, secondary involves hydrogen bonding into shapes like alpha helices and beta sheets, tertiary is the 3D folding of these structures, and quaternary involves the assembly of multiple protein subunits. Proteins serve as enzymes, hormones, antibodies, and structures. They undergo synthesis from amino acids and breakdown through catabolism. Disorders can occur if amino acid metabolism is disrupted.
Chemistry of proteins
Proteins are composed of chains of amino acids and serve important structural and functional roles in biology. They can be classified based on their composition, structure, and biological function. Common analytical techniques used to study proteins include chromatography, electrophoresis, and mass spectrometry which separate proteins based on properties like size and charge. The diversity of amino acid side chains allows proteins to adopt complex 3D structures and perform a wide variety of critical roles in the body.
Viewers also liked (8)
B.Sc. Biochem II Biomolecule I U 3.2 Classification of Protein & Denaturation
B.Sc. Biochem II Biomolecule I U 3.2 Classification of Protein & Denaturation
Similar to Proteins
PROTEINS GROUP 2.pptx
This presentation discusses proteins and their functions. It defines proteins as nitrogenous compounds made of amino acids. Proteins perform many crucial functions in the body including growth, enzyme production, transport, defense, and maintenance of acid-base balance. The presentation covers protein structure, classification, sources, digestion and absorption. It emphasizes the importance of consuming complete proteins from both plant and animal sources to meet nutritional needs. Recommended daily intakes vary by age, gender and physiological state. Maintaining positive nitrogen balance is also discussed.
Metabolism of Amino Acids
This document provides information on the composition and metabolism of amino acids and proteins. It discusses the following key points:
- Proteins are made up of chains of amino acids and are essential components of cells, enzymes, and genes. They perform many important functions in the body.
- There are three main classifications of proteins: simple proteins, conjugated proteins, and derived proteins. Simple proteins include albumins, globulins, and histones. Conjugated proteins are composed of simple proteins combined with other substances. Derived proteins result from partial or complete hydrolysis of other proteins.
- Amino acids are the building blocks of proteins. There are over 500 known amino acids but only 20 that are used in
Classification of Protein.pdf
The document classifies proteins based on their solubility, shape, composition, and function. It discusses several classifications:
1. Based on solubility and composition, proteins are divided into simple, conjugated, and derived groups. Simple proteins include albumins, globulins, prolamins, glutelins, and others.
2. Based on function, proteins serve as enzymes, hormones, antibodies, storage, transport, toxic, structural, contractile, and secretory functions.
3. Amino acids are the building blocks of proteins. They are classified based on properties like polarity, nutritional requirements, and side chain groups. Peptide bonds form between amino acids and are characterized by their rigidity
PROTEINS.pptx
This document discusses proteins, including their definition, structure, classification, and roles in the body. It begins by defining proteins as complex molecules composed of amino acids joined by peptide bonds. It then discusses protein structure, including primary, secondary, tertiary, and quaternary levels. Proteins are classified based on solubility, composition, function, shape, and size. They play many important roles such as enzymatic catalysis, regulation, protection, storage, transport, structure, and contraction. The document provides a detailed overview of the nature and importance of proteins.
Proteins PPT final (1).pptx
Proteins are polymers of amino acids that perform essential functions in living organisms. They can be classified as simple, conjugated, or derived proteins based on their structure and components. Simple proteins like albumins and globulins are made of amino acids alone, while conjugated proteins also contain non-protein elements like nucleic acids or carbohydrates. Proteins have primary, secondary, tertiary, and quaternary levels of structure that determine their shape and function. They are found in all tissues and play critical roles including structure, movement, digestion, energy storage, and heredity.
Protein 26 32
The document discusses proteins and amino acids. It describes that proteins are composed of amino acids, which are the monomers that make up proteins. There are 20 standard amino acids that combine to form various protein structures. The document then classifies proteins based on their shape, size, solubility, physical properties and functions. It provides examples of different types of proteins like keratins, collagens, globulins, and histones. The composition and importance of proteins is also summarized.
Protein & Biochemical Role part 2
Proteins play many important biochemical roles in the body. They act as enzymes, hormones, antibodies, and structural components. Proteins can be classified based on their shape (fibrous or globular) or chemical composition (simple or conjugated). Simple proteins only contain amino acids, while conjugated proteins also contain non-amino acid groups like nucleic acids, lipids, carbohydrates, or metals. Proteins are further classified as complete or incomplete based on whether they contain all essential amino acids.
Plasma Proteins important and brief notes
This document discusses plasma proteins, including their types, functions, biosynthesis, and degradation. It covers the main plasma proteins such as albumin, globulins, immunoglobulins, acute phase reactants, and others. Albumin is the major plasma protein that helps maintain colloidal osmotic pressure and transports substances throughout the body. Globulins include proteins involved in blood clotting, iron transport, and immune responses. Immunoglobulins are antibodies that provide antibody-mediated immunity. Levels of acute phase reactants increase or decrease during inflammation.
proteins.pptx
This document provides an overview of proteins, including their classification. It begins by stating that proteins are the most abundant biomolecules in living systems and are required for growth, structure, and function. The document then discusses that proteins are polymers of amino acids. It provides examples of how proteins serve as structural elements and building blocks. The main body covers different classifications of proteins, including simple/holo proteins classified by solubility, complex/conjugated proteins which contain non-amino acid groups, and derived proteins from enzymatic breakdown. In closing, it thanks the reader and provides institution details.
P R O T E I N S
Proteins are composed of amino acids and are essential macronutrients that serve important structural and functional roles in the body. They are classified based on solubility and properties into simple, conjugated, and derived proteins and play roles like protection, movement, catalysis, signaling, structure, storage, and transport. The 20 standard amino acids that make up proteins are either essential or non-essential, with essential amino acids needing to be obtained through diet.
Cell & Homeostasis
Human physiology is the study of the normal functions and mechanisms of human organs and body systems, including how cells, muscles, and organs work together and interact. The cell is the basic structural and functional unit of the body. The plasma membrane forms the outer surface of the cell and acts as a selective barrier, separating the internal and external environments according to the fluid mosaic model. It consists of a bilayer of phospholipids, cholesterol, and proteins embedded within this lipid bilayer.
Protein.pdf
Proteins serve many important functions in the body. They come in different sizes and shapes to carry out specific roles like structure, regulation, and energy. Main protein functions include providing structure to tissues like bone, skin, and muscle through proteins like actin, collagen, and keratin. Enzymes are protein regulators that allow the body to break down food and perform metabolic processes. Hormones are chemical messenger proteins that coordinate bodily processes. Proteins also transport molecules, play roles in fluid and pH balance through proteins like albumin and hemoglobin, and provide immune defense against pathogens. Each amino acid monomer that makes up proteins also has distinct functions important for growth, metabolism, nerve signaling, and other processes.
Lec.3protein chem.classification new microsoft powerpoint presentation
Proteins are complex biomolecules composed of amino acid chains that perform essential functions in the human body. They can be classified based on their composition, structure, and function. Some key types of proteins include structural proteins like collagen and keratin; transport proteins like hemoglobin; catalytic proteins which include enzymes; and regulatory proteins such as hormones. There are approximately 50,000 to 200,000 different proteins present in the human body, performing vital roles such as oxygen transport, muscle movement, immune defense, and metabolic processes.
Lec.3 protein chem.classification
Proteins are complex biomolecules composed of amino acid chains that perform essential functions in the human body. They can be classified based on their composition, structure, and function. Some key types of proteins include structural proteins like collagen and keratin; transport proteins like hemoglobin; catalytic proteins which include enzymes; and regulatory proteins such as hormones. There are approximately 50,000 to 200,000 different proteins present in the human body, performing vital roles such as oxygen transport, muscle movement, immune defense, and metabolic processes.
The Physiological role of cell organelles.pptx
This document discusses the physiological roles of various cell organelles, including the cell membrane, nucleus, endoplasmic reticulum, Golgi apparatus, lysosomes, mitochondria, peroxisomes, and cytoskeleton. It describes the composition and functions of the cell membrane, including transport processes. The roles of other organelles like the nucleus, endoplasmic reticulum, Golgi apparatus and lysosomes in processes like protein synthesis, lipid synthesis, packaging and secretion of materials are covered. The document also discusses the structure and functions of mitochondria, peroxisomes and components of the cytoskeleton.
PROTEINS LECTURE_1.ppt
Proteins are complex organic compounds composed of amino acids linked by peptide bonds. They come in many forms and have a wide diversity of functions. Proteins can be classified based on their structure, composition, solubility and functions. The main types include simple proteins like albumins and globulins, conjugated proteins which combine with non-protein groups, and derived proteins formed by hydrolysis of other proteins. Proteins play critical roles in the body as enzymes, structures, nutrients, and more.
protein classification and it's properties
This document provides an introduction and overview of protein classification and properties. It discusses how proteins are classified based on their source, shape, composition and solubility, as well as their biological functions. Key points include that proteins are composed of amino acids and can have globular or fibrous shapes. Conjugated proteins are linked to non-protein groups. Insulin is an important protein hormone that regulates blood sugar levels and was the first to be fully sequenced. The document also examines general protein properties like molecular weight and reactions involving amino acid groups.
Functional classification of proteins- -pry, sec, tert, and quartenary- struc...
Proteins are essential components of living organisms that are made up of amino acids. They perform many important functions in the body including structure, movement, regulation, and transport. Proteins have a primary structure defined by their amino acid sequence and can form secondary structures like alpha helices or beta sheets through hydrogen bonding between amino acids in the chain. Their structure determines their diverse functions in the body.
Proteins digestion, absorption, and metabolism
Proteins are made of amino acids and have primary, secondary, tertiary, and quaternary levels of structure. They perform many essential functions in the body. Protein digestion begins in the stomach through the actions of gastric acid and the enzyme pepsin. Pepsin breaks proteins into smaller polypeptides and proteoses. In the small intestine, pancreatic enzymes and bile further break down polypeptides into dipeptides and free amino acids which can then be absorbed.
biological molecules.pdf
The document discusses the major classes of biological molecules that are important for living things: carbohydrates, lipids, and proteins. Carbohydrates include monosaccharides, disaccharides, and polysaccharides and function for energy storage and structure. Lipids are nonpolar and include fatty acids, neutral fats, phospholipids, and steroids that function for energy storage, cell membrane structure, and vitamins/hormones. Proteins are polymers of amino acids joined by peptide bonds and have diverse functions including enzymes, defense, transport, structure, and regulation.
Similar to Proteins (20)
Lec.3protein chem.classification new microsoft powerpoint presentation
Lec.3protein chem.classification new microsoft powerpoint presentation
Functional classification of proteins- -pry, sec, tert, and quartenary- struc...
Functional classification of proteins- -pry, sec, tert, and quartenary- struc...
More from Kinza Ayub
Tertiary structure of proteins
Tertiary structure describes how protein chains fold upon themselves into complex 3D shapes. These shapes are stabilized by interactions between amino acid side chains like disulfide bonds, hydrogen bonds, and hydrophobic interactions. Long protein chains often contain multiple domains that fold independently. Quaternary structure refers to complexes of two or more protein subunits. Chaperone proteins assist other proteins in proper folding, while misfolded proteins can accumulate and cause diseases.
Primary structure of proteins
The document discusses the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the specific sequence of amino acids that make up the protein. Peptide bonds form between the amino acids, linking an amino group of one to the carboxyl group of the other. These peptide bonds can be broken down by strong acids or bases at high temperatures through a non-enzymatic process called hydrolysis.
Plasma proteins
The plasma is the liquid portion of blood that contains proteins like albumins, globulins, fibrinogen, and immunoglobulins. The main classes of globulins are alpha, beta, and gamma globulins. Immunoglobulins, also called antibodies, are gamma globulins that recognize and bind to antigens with high specificity. The five major classes of immunoglobulins in humans are IgG, IgM, IgA, IgD, and IgE, which have different structures and functions. Multiple myeloma is a cancer of plasma cells that results in overproduction of a single immunoglobulin class.
Immunoglobulins 2001
Immunoglobulins are glycoprotein molecules produced by plasma cells in response to antigens that function as antibodies. They have a basic structure consisting of two heavy chains and two light chains held together by disulfide bonds, forming variable and constant regions. The variable regions determine antigen binding specificity, while the constant regions determine effector functions. The five major classes in humans are IgG, IgM, IgA, IgD, and IgE, which have different structures, properties, and functions in the immune response.
Fibrous proteins
Collagen and elastin are fibrous proteins that provide structure in the body. Collagen forms a rigid triple helix structure made of three polypeptide chains. It is abundant in skin, bone, and cartilage. Elastin provides elasticity and is found in lungs, arteries, and ligaments. Both proteins derive their mechanical properties from their unique secondary and tertiary structures, which are stabilized by interactions between amino acid side chains.
Fibrous proteins
Collagen and elastin are fibrous proteins that provide structure in the body. Collagen forms a rigid triple helix structure made of three polypeptide chains. It is abundant in skin, bone, and cartilage. Elastin provides elasticity and is found in lungs, arteries, and ligaments. Both proteins derive their mechanical properties from their unique secondary and tertiary structures, which are stabilized by interactions between amino acid side chains.
Digestion and absorption of proteins
The document discusses protein digestion and absorption. Proteins are broken down into peptides and amino acids by digestive enzymes in the stomach and small intestine. Peptides and amino acids are then absorbed into the bloodstream. Most proteins must be fully broken down before absorption, though some intact proteins can be absorbed by infants or through abnormal routes in adults. The amino acids are used throughout the body for protein synthesis, energy production, and other purposes.
Amino acid and_protein_chemistery
Proteins are the most abundant and functionally diverse molecules in living systems, composed of amino acids linked by peptide bonds. They can be classified in various ways, including by molecular structure (globular vs fibrous), solubility, presence of non-protein groups, function (enzymes, hormones, etc.), and nutritional quality. The 20 primary amino acids are the building blocks of all proteins in plants and animals.
Amino acids&proteins
Amino acids are the building blocks of proteins. They contain amino and carboxyl groups and a side chain, and are joined together via peptide linkages. Amino acids exist in two forms - D and L - but the L-form is used in proteins. They are soluble in water but insoluble in fat, and at physiologic pH the carboxyl group is negatively charged while the amino group is positively charged.
Amino acid and protein chemistery
Proteins are the most abundant and functionally diverse molecules in living systems, composed of amino acids linked by peptide bonds. They can be classified in various ways, including by molecular structure (globular vs fibrous), solubility, presence of non-protein groups, function (enzymes, hormones, etc.), and nutritional quality. The 20 primary amino acids are the building blocks of all proteins in plants and animals, and each has a specific genetic codon in mRNA.
More from Kinza Ayub (10)
Proteins
- 1. Proteins Derived from the Greek word protos that means I occupy
- 2. Importanance • Take an essential part in the formation Of protoplasm. • Nucleoproteins which are complexes of • Proteins with nucleic acid serve as carriers of heredity. • Enzymes are protein • Proteins are an integral part of all viruses
- 3. • One gram of protein furnishes 4.1 kilocalories • Have specialized functions e.g. hemoglobin, hormone • Present in blood plasma as colloidal particle • Plasma protein take part in blood coagulation
- 4. • Antibodies are proteins • Act as transporting or carrier molecule • Make complexes with carbohydrates and Lipids.
- 5. Classification • Physico-chemical classification • Functional classification • Structural classification
- 6. Physico-chemical classification • Simple proteins • Compound proteins • Derived proteins
- 7. Simple proteins • Albumin • Globulin • Globin • Prolamin • Histones • Protamin • Albuminoids: keratin ,collagen ,elastin