A QUICK GLANCE AT PROTEIN STRUCTURE
•Download as PPT, PDF•
2 likes•1,152 views
Proteins have four levels of structure - primary, secondary, tertiary, and quaternary - that determine their function. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structures form due to hydrogen bonding within the chain, resulting in alpha helices or beta pleated sheets. Tertiary structure describes the overall 3D shape of the protein formed by interactions between amino acid side chains. Quaternary structure involves interactions between multiple polypeptide subunits.
Report
Share
Report
Share
![Introduction ,[object Object],[object Object],[object Object],[object Object],[object Object],[object Object]](data:image/gif;base64,R0lGODlhAQABAIAAAAAAAP///yH5BAEAAAAALAAAAAABAAEAAAIBRAA7)
Recommended
Phys 02 13
There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. The secondary structure involves hydrogen bonds forming coils, sheets, or loops. Tertiary structure is the packing of these secondary structures into domains. Quaternary structure involves multiple proteins combining. A protein's shape determines its function, and denaturation can destroy this shape and impair function.
Protein structure & function
Proteins fold into their functional three-dimensional shapes due to interactions between the amino acid side chains. The primary structure of a protein is its amino acid sequence, while secondary structures like alpha helices and beta sheets form due to hydrogen bonds within the peptide backbone. Tertiary structure is determined by non-covalent interactions between the side chains that stabilize the overall three-dimensional structure of the protein. Quaternary structure refers to the interaction between multiple polypeptide subunits in a single protein.
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
Protein structures by anivjeh
tertiary and quaternary structures of protein molecules
how long chain of amino acids (polypeptide) gets converted in to protein molecules
Proteins
Proteins are made up of chains of amino acids that form various structures which determine the protein's function. The amino acid sequence forms the primary structure. Hydrogen bonding forms regular patterns of alpha helices and beta sheets as the secondary structure. Tertiary structure is the final 3D shape from hydrophobic interactions. Some proteins have quaternary structure as complexes of multiple polypeptide chains.
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.
Amino acids of biological importance 2021
This document discusses amino acids and proteins of biological importance. It defines amino acids as organic acids that contain one or more amino groups. Proteins are formed from chains of 50 or more amino acids linked by peptide bonds. The document classifies amino acids and discusses the structures of proteins including primary, secondary, tertiary and quaternary structure. It also addresses the denaturation and conformational classification of proteins.
Introduction to protein and classification by sohail
This document provides an introduction and overview of protein structure and classification. It discusses the basic building blocks of proteins, the four levels of protein structure (primary, secondary, tertiary, and quaternary), and two main methods of protein classification - by shape (globular vs. fibrous proteins) and by function (enzymes, hormones, structural proteins, etc.). The document aims to cover key concepts about protein structure and organization in a comprehensive yet concise manner.
Recommended
Phys 02 13
There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. The secondary structure involves hydrogen bonds forming coils, sheets, or loops. Tertiary structure is the packing of these secondary structures into domains. Quaternary structure involves multiple proteins combining. A protein's shape determines its function, and denaturation can destroy this shape and impair function.
Protein structure & function
Proteins fold into their functional three-dimensional shapes due to interactions between the amino acid side chains. The primary structure of a protein is its amino acid sequence, while secondary structures like alpha helices and beta sheets form due to hydrogen bonds within the peptide backbone. Tertiary structure is determined by non-covalent interactions between the side chains that stabilize the overall three-dimensional structure of the protein. Quaternary structure refers to the interaction between multiple polypeptide subunits in a single protein.
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
Protein structures by anivjeh
tertiary and quaternary structures of protein molecules
how long chain of amino acids (polypeptide) gets converted in to protein molecules
Proteins
Proteins are made up of chains of amino acids that form various structures which determine the protein's function. The amino acid sequence forms the primary structure. Hydrogen bonding forms regular patterns of alpha helices and beta sheets as the secondary structure. Tertiary structure is the final 3D shape from hydrophobic interactions. Some proteins have quaternary structure as complexes of multiple polypeptide chains.
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.
Amino acids of biological importance 2021
This document discusses amino acids and proteins of biological importance. It defines amino acids as organic acids that contain one or more amino groups. Proteins are formed from chains of 50 or more amino acids linked by peptide bonds. The document classifies amino acids and discusses the structures of proteins including primary, secondary, tertiary and quaternary structure. It also addresses the denaturation and conformational classification of proteins.
Introduction to protein and classification by sohail
This document provides an introduction and overview of protein structure and classification. It discusses the basic building blocks of proteins, the four levels of protein structure (primary, secondary, tertiary, and quaternary), and two main methods of protein classification - by shape (globular vs. fibrous proteins) and by function (enzymes, hormones, structural proteins, etc.). The document aims to cover key concepts about protein structure and organization in a comprehensive yet concise manner.
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.
Structure of protein
This document summarizes the four levels of protein structure: primary, secondary, tertiary, and quaternary. It provides details on each level: primary structure refers to the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding between amino acids to form regular structures like alpha helices and beta pleated sheets. Tertiary structure describes the overall 3D shape of the protein arising from secondary structures. Quaternary structure involves interactions between two or more polypeptide chains, as seen in hemoglobin which is made of four polypeptide subunits.
Nucleic Acids
DNA and RNA are nucleic acids that carry genetic information. DNA stores and transmits information through generations, while RNA assists in protein synthesis. Nucleic acids are made up of nucleotides, which consist of a sugar, phosphate group, and nitrogenous base. The bases on DNA and RNA pair up through hydrogen bonding to form the double helix structure of DNA or single strands of RNA. Polymerase enzymes are necessary to copy DNA through replication and transcribe DNA into RNA through transcription.
Peptide+structure
The document discusses various aspects of peptide structure and function including:
1. The common secondary structural motifs of peptides including alpha helices, beta sheets, beta turns, and random coils.
2. Techniques used to study peptide conformation such as crystallography, NMR, and CD spectroscopy.
3. Factors that influence peptide structure including amino acid sequence, solvent environment, and intermolecular interactions.
PROTEIN STRUCTURE PRESENTATION
The document discusses the structure of proteins at various levels of organization:
- Proteins are composed of amino acids linked together by peptide bonds to form polypeptide chains. The sequence and interactions of these chains determine the protein's structure.
- There are four levels of protein structure - primary, secondary, tertiary, and quaternary. Secondary structure includes alpha helices and beta sheets formed by hydrogen bonding between amino acids in the chain. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure involves the interaction of multiple polypeptide chains.
- Protein structure enables proteins to perform their diverse functions through processes like enzyme catalysis, oxygen transport, and providing structure
Protein structure
This document discusses the primary, secondary, tertiary, and quaternary structures of proteins. It defines each structure and provides examples. Primary structure refers to the sequence of amino acids in the polypeptide chain. Secondary structures include the alpha helix, beta pleated sheet, and triple helix. Tertiary structure describes the overall 3D shape of a protein formed by interactions between amino acid R groups. Quaternary structure involves proteins with two or more polypeptide chains. The document also covers protein hydrolysis, which breaks peptide bonds, and denaturation, which disrupts higher-order protein structures.
Proteins - Edexcel A-Level Biology B Topic 1.2
This document discusses proteins and their structure. It notes that proteins make up 18% of the human body and are essential components of things like hair, skin, nails, enzymes, hormones, muscles and more. Proteins are composed of long chains of amino acids that join together via condensation reactions. There are 20 naturally occurring amino acids that can combine in various ways to form different proteins. The chains of amino acids fold into complex 3D structures held together by bonds like peptide bonds, hydrogen bonds, disulfide bonds, and ionic bonds. This intricate 3D structure allows proteins to perform their many vital functions in the body.
BT631-4-peptide_bonds
The peptide bond forms spontaneously via a condensation reaction that releases a small molecule like water. It has partial double bond character that restricts rotation, resulting in planar geometry. The phi and psi angles of the peptide backbone determine its conformation within allowed regions of the Ramachandran plot, avoiding steric clashes. While most peptide bonds adopt the trans configuration, proline favors cis. Protein function arises from its precise three-dimensional structure.
Protein structure
Protein structure can be described at several levels of organization. The primary structure is the amino acid sequence, while the secondary structure describes local patterns like alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure refers to the overall 3D shape of a single polypeptide chain. Quaternary structure involves the arrangement of multiple protein subunits. Together these organizational levels allow proteins to carry out their diverse functions in the cell.
Protein structure
- Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure is the 3D shape formed by interactions between different parts of the polypeptide. Quaternary structure refers to the assembly of multiple polypeptide subunits.
Seminar on protein and protein structure
Seminar on protein and protein structureB V V S Hanagal Shri Kumareshwar College of Pharmacy, Bagalkote
The document discusses the four levels of structural organization of proteins: primary, secondary, tertiary, and quaternary structure. It describes the primary structure as the linear sequence of amino acids in a protein. Secondary structures form due to hydrogen bonding and include alpha helices and beta sheets. Tertiary structure refers to the three dimensional folding of a protein chain. Quaternary structure occurs when multiple protein chains combine to form a functional protein. The document focuses on different types of secondary structures like alpha helices, beta sheets, loops, and turns.Organic molecules
Early experiments by Stanley Miller showed that organic molecules like amino acids could form from simple molecules like methane, ammonia and hydrogen with energy from heat and electricity. More recent experiments have found that amino acids and other organic molecules form easily under these conditions, suggesting this could have been how the first organic molecules formed on early Earth before the emergence of life. Proteins are made of amino acids linked together in chains that then fold into complex 3D shapes determined by interactions between their variable side chains. This folding allows proteins to perform a huge variety of functions in living cells and organisms.
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.
Proteins and nucleic acids 2014
Proteins and nucleic acids are important macromolecules that make up cells. Proteins are composed of amino acids and perform critical functions like structure and catalysis. The four levels of protein structure are primary, secondary, tertiary, and quaternary. Nucleic acids DNA and RNA contain nitrogenous bases and sugars. DNA provides genetic instructions and replicates, while RNA has roles in protein synthesis. ATP is an energy-carrying molecule made from RNA nucleotides.
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.
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.
Strutural organisation of proteins
The document discusses the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the peptide chain. The secondary structure involves hydrogen bonding that causes the chain to fold into structures like alpha helices or beta sheets. Tertiary structure describes further folding and interactions that result in the protein's three-dimensional shape. Quaternary structure refers to multiple peptide chains linked together in a protein.
Biochemistry - Ch4 protein structure , and function
This document discusses the structure of proteins at multiple levels. It explains that a protein's amino acid sequence determines its 3D structure, and its structure dictates its function. Noncovalent interactions like hydrogen bonds, hydrophobic interactions, and electrostatic interactions are important forces that stabilize a protein's native structure. The peptide bond is rigid and planar, limiting the possible conformations of the polypeptide backbone. Common secondary structures like alpha helices and beta sheets form due to favorable hydrogen bonding patterns between peptide bonds.
Polypeptides of defined sequence
Proteins are polypeptides with a defined sequence of amino acids. Each protein's sequence is determined by instructions contained in the cell's genetic material, which specifies which of the 20 standard amino acids make up the protein and in what order. This precise sequence defines the protein's structure and function.
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.
Transcription notes
Protein is made from amino acids that interact through bonding and folding. Proteins control traits like hair and skin color through the amount of melanin present. Blood carries oxygen using the protein hemoglobin. DNA contains genes and remains in the nucleus, while messenger RNA (mRNA) acts as an intermediary, traveling between the nucleus and cytoplasm to create proteins. Transcription involves DNA unzipping and mRNA being built from the DNA template. Translation occurs when mRNA leaves the nucleus and attaches to ribosomes to recruit transfer RNA (tRNA) and amino acids to build a protein chain.
Protien Metabolism
The structure of a protein determines its function. For enzymes, the binding site or active site allows substrates to bind via lock-and-key or induced fit mechanisms. Myoglobin and hemoglobin both contain heme groups to bind oxygen, but differ in structure - myoglobin is spherical while hemoglobin is a tetramer. This allows hemoglobin to exhibit cooperative binding and transport oxygen more efficiently than myoglobin via conformational changes.
More Related Content
What's hot
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.
Structure of protein
This document summarizes the four levels of protein structure: primary, secondary, tertiary, and quaternary. It provides details on each level: primary structure refers to the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding between amino acids to form regular structures like alpha helices and beta pleated sheets. Tertiary structure describes the overall 3D shape of the protein arising from secondary structures. Quaternary structure involves interactions between two or more polypeptide chains, as seen in hemoglobin which is made of four polypeptide subunits.
Nucleic Acids
DNA and RNA are nucleic acids that carry genetic information. DNA stores and transmits information through generations, while RNA assists in protein synthesis. Nucleic acids are made up of nucleotides, which consist of a sugar, phosphate group, and nitrogenous base. The bases on DNA and RNA pair up through hydrogen bonding to form the double helix structure of DNA or single strands of RNA. Polymerase enzymes are necessary to copy DNA through replication and transcribe DNA into RNA through transcription.
Peptide+structure
The document discusses various aspects of peptide structure and function including:
1. The common secondary structural motifs of peptides including alpha helices, beta sheets, beta turns, and random coils.
2. Techniques used to study peptide conformation such as crystallography, NMR, and CD spectroscopy.
3. Factors that influence peptide structure including amino acid sequence, solvent environment, and intermolecular interactions.
PROTEIN STRUCTURE PRESENTATION
The document discusses the structure of proteins at various levels of organization:
- Proteins are composed of amino acids linked together by peptide bonds to form polypeptide chains. The sequence and interactions of these chains determine the protein's structure.
- There are four levels of protein structure - primary, secondary, tertiary, and quaternary. Secondary structure includes alpha helices and beta sheets formed by hydrogen bonding between amino acids in the chain. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure involves the interaction of multiple polypeptide chains.
- Protein structure enables proteins to perform their diverse functions through processes like enzyme catalysis, oxygen transport, and providing structure
Protein structure
This document discusses the primary, secondary, tertiary, and quaternary structures of proteins. It defines each structure and provides examples. Primary structure refers to the sequence of amino acids in the polypeptide chain. Secondary structures include the alpha helix, beta pleated sheet, and triple helix. Tertiary structure describes the overall 3D shape of a protein formed by interactions between amino acid R groups. Quaternary structure involves proteins with two or more polypeptide chains. The document also covers protein hydrolysis, which breaks peptide bonds, and denaturation, which disrupts higher-order protein structures.
Proteins - Edexcel A-Level Biology B Topic 1.2
This document discusses proteins and their structure. It notes that proteins make up 18% of the human body and are essential components of things like hair, skin, nails, enzymes, hormones, muscles and more. Proteins are composed of long chains of amino acids that join together via condensation reactions. There are 20 naturally occurring amino acids that can combine in various ways to form different proteins. The chains of amino acids fold into complex 3D structures held together by bonds like peptide bonds, hydrogen bonds, disulfide bonds, and ionic bonds. This intricate 3D structure allows proteins to perform their many vital functions in the body.
BT631-4-peptide_bonds
The peptide bond forms spontaneously via a condensation reaction that releases a small molecule like water. It has partial double bond character that restricts rotation, resulting in planar geometry. The phi and psi angles of the peptide backbone determine its conformation within allowed regions of the Ramachandran plot, avoiding steric clashes. While most peptide bonds adopt the trans configuration, proline favors cis. Protein function arises from its precise three-dimensional structure.
Protein structure
Protein structure can be described at several levels of organization. The primary structure is the amino acid sequence, while the secondary structure describes local patterns like alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure refers to the overall 3D shape of a single polypeptide chain. Quaternary structure involves the arrangement of multiple protein subunits. Together these organizational levels allow proteins to carry out their diverse functions in the cell.
Protein structure
- Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure is the 3D shape formed by interactions between different parts of the polypeptide. Quaternary structure refers to the assembly of multiple polypeptide subunits.
Seminar on protein and protein structure
Seminar on protein and protein structureB V V S Hanagal Shri Kumareshwar College of Pharmacy, Bagalkote
The document discusses the four levels of structural organization of proteins: primary, secondary, tertiary, and quaternary structure. It describes the primary structure as the linear sequence of amino acids in a protein. Secondary structures form due to hydrogen bonding and include alpha helices and beta sheets. Tertiary structure refers to the three dimensional folding of a protein chain. Quaternary structure occurs when multiple protein chains combine to form a functional protein. The document focuses on different types of secondary structures like alpha helices, beta sheets, loops, and turns.Organic molecules
Early experiments by Stanley Miller showed that organic molecules like amino acids could form from simple molecules like methane, ammonia and hydrogen with energy from heat and electricity. More recent experiments have found that amino acids and other organic molecules form easily under these conditions, suggesting this could have been how the first organic molecules formed on early Earth before the emergence of life. Proteins are made of amino acids linked together in chains that then fold into complex 3D shapes determined by interactions between their variable side chains. This folding allows proteins to perform a huge variety of functions in living cells and organisms.
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.
Proteins and nucleic acids 2014
Proteins and nucleic acids are important macromolecules that make up cells. Proteins are composed of amino acids and perform critical functions like structure and catalysis. The four levels of protein structure are primary, secondary, tertiary, and quaternary. Nucleic acids DNA and RNA contain nitrogenous bases and sugars. DNA provides genetic instructions and replicates, while RNA has roles in protein synthesis. ATP is an energy-carrying molecule made from RNA nucleotides.
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.
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.
Strutural organisation of proteins
The document discusses the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the peptide chain. The secondary structure involves hydrogen bonding that causes the chain to fold into structures like alpha helices or beta sheets. Tertiary structure describes further folding and interactions that result in the protein's three-dimensional shape. Quaternary structure refers to multiple peptide chains linked together in a protein.
Biochemistry - Ch4 protein structure , and function
This document discusses the structure of proteins at multiple levels. It explains that a protein's amino acid sequence determines its 3D structure, and its structure dictates its function. Noncovalent interactions like hydrogen bonds, hydrophobic interactions, and electrostatic interactions are important forces that stabilize a protein's native structure. The peptide bond is rigid and planar, limiting the possible conformations of the polypeptide backbone. Common secondary structures like alpha helices and beta sheets form due to favorable hydrogen bonding patterns between peptide bonds.
Polypeptides of defined sequence
Proteins are polypeptides with a defined sequence of amino acids. Each protein's sequence is determined by instructions contained in the cell's genetic material, which specifies which of the 20 standard amino acids make up the protein and in what order. This precise sequence defines the protein's structure and function.
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.
What's hot (20)
Biochemistry - Ch4 protein structure , and function
Biochemistry - Ch4 protein structure , and function
Viewers also liked
Transcription notes
Protein is made from amino acids that interact through bonding and folding. Proteins control traits like hair and skin color through the amount of melanin present. Blood carries oxygen using the protein hemoglobin. DNA contains genes and remains in the nucleus, while messenger RNA (mRNA) acts as an intermediary, traveling between the nucleus and cytoplasm to create proteins. Transcription involves DNA unzipping and mRNA being built from the DNA template. Translation occurs when mRNA leaves the nucleus and attaches to ribosomes to recruit transfer RNA (tRNA) and amino acids to build a protein chain.
Protien Metabolism
The structure of a protein determines its function. For enzymes, the binding site or active site allows substrates to bind via lock-and-key or induced fit mechanisms. Myoglobin and hemoglobin both contain heme groups to bind oxygen, but differ in structure - myoglobin is spherical while hemoglobin is a tetramer. This allows hemoglobin to exhibit cooperative binding and transport oxygen more efficiently than myoglobin via conformational changes.
project proposal presentation a comparative study
This project proposal compares the nutrients in foods cooked conventionally versus in the microwave. The hypothesis is that there will be a significant nutritional difference between the cooking methods. Samples of soybeans, cabbage, greens and potatoes will be cooked both conventionally and in the microwave. Proteins, carbohydrates, and vitamin C will then be extracted from the processed foods and tested quantitatively using specific reagents. Spectrophotometry will be used to test for proteins. The results will be analyzed to either reject or accept the hypothesis that there is a nutritional difference depending on the cooking method.
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.
Protein structure
This document provides an overview of protein structure from primary to quaternary levels. It discusses the building blocks of proteins including amino acids and peptide bonds. Secondary structures like alpha helices and beta sheets are explained. Tertiary structure refers to the global folding of the protein chain. Quaternary structure involves the assembly of multiple protein subunits. Examples are given of protein complexes demonstrating tertiary and quaternary levels of structure. The document also outlines different classes of proteins based on function, structure, and cellular localization.
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.
Viewers also liked (6)
Similar to A QUICK GLANCE AT PROTEIN STRUCTURE
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
Proteins (2)
Proteins are macromolecules composed of amino acid chains. They have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structure involves local folding into structures like alpha helices and beta sheets. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure refers to the shape of proteins made of multiple polypeptide subunits. Proteins serve many important functions and can be classified based on their structure, composition, or function.
chemistry of protein.ppt
Protein is made up of amino acids joined together by peptide bonds. There are 20 standard amino acids that make up proteins. Proteins have primary, secondary, tertiary, and sometimes quaternary structures that give them their shapes. The primary structure is the linear sequence of amino acids, secondary structures include alpha helices and beta sheets, tertiary structure is the 3D shape of the protein, and quaternary refers to multiple protein subunits.
Protein and Its structure
Proteins are made up of amino acids linked together through 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 structure involves local folding into structures like alpha helices and beta sheets. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure occurs when multiple protein subunits assemble to form an oligomeric complex.
Structure and function of protein
This document is a presentation on molecular biology given by Mujeeb Ur Rehman to Dr. Abid Jan. It discusses the key topics of proteins, amino acids, and protein structure. Specifically, it covers the 20 standard amino acids, how they are classified, and how they come together to form the primary, secondary, tertiary, and quaternary structures of proteins through covalent and non-covalent bonds. Forces like hydrogen bonds, ionic bonds, and hydrophobic interactions contribute to stable protein folding and structure formation at each level.
Introduction to Proteins and Aminoacids with Clinical significance
This document discusses proteins, including their structure and properties. It provides definitions of key protein terms like amino acids, peptides, and the four levels of protein structure - primary, secondary, tertiary, and quaternary. It also summarizes factors that can cause protein denaturation, like heat, acids, bases, and alcohol, disrupting the shapes and bonds of protein molecules. Food sources of protein from both animal and plant sources are listed.
Biol161 02
The document discusses the key biomolecules found in living things including proteins, carbohydrates, lipids, and nucleic acids. It describes the basic monomers like amino acids and nucleotides that make up these biomolecules, and how they are linked together through peptide bonds in proteins or phosphodiester bonds in nucleic acids. It also provides examples of specific biomolecules like collagen, hemoglobin, and fatty acids to illustrate their structures and functions.
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.
Amino Acids and Protein
Study Material for B.Sc. Students
Primary, secondary, tertiary, quaternary structures of protein, motiffs and domains, subunits
Proteins.
Proteins are composed of amino acids and have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves local folding into patterns like alpha helices and beta sheets. Tertiary structure is the overall three-dimensional shape formed by interactions between different parts of the polypeptide chain. Quaternary structure refers to the shape of proteins with multiple polypeptide subunits. Proteins perform many important functions in the body as enzymes, antibodies, hormones, and structural components.
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.
Amino acids and protein
Amino acids are organic compounds containing amino and carboxylic acid groups. There are about 300 amino acids in nature but only 20 are found in proteins. Amino acids are linked together via peptide bonds to form polypeptide chains and proteins. There are four levels of protein structure - primary, secondary, tertiary, and quaternary - that determine a protein's shape and function. Proteins can be classified as simple proteins which break down into amino acids, or conjugated proteins which break down into a protein and non-protein component like lipids or carbohydrates.
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.
Protien
This document provides information about proteins. It begins with an introduction stating that proteins are abundant organic molecules that are found in all parts of cells and make up about 50% of cellular dry weight. It then discusses the origin of the word "protein" and the elemental composition of proteins. The document outlines the bonds responsible for protein structure, including peptide bonds, disulfide bonds, and non-covalent bonds. It describes the four levels of protein structure - primary, secondary, tertiary, and quaternary. Key properties of proteins and methods of determining protein structure are summarized. The document concludes by discussing clinical aspects of proteins, including prion diseases and Alzheimer's disease.
Proteins
Proteins are essential macromolecules that make up 20% of the human body. They are composed of amino acids and perform many critical functions including structure, regulation, catalysis, movement and more. Protein synthesis occurs in ribosomes within cells. Proteins are not stored but are broken down if excess amino acids are consumed. They have primary, secondary, tertiary and quaternary levels of structure determined by amino acid sequence and interactions. There are 20 standard amino acids that are linked by peptide bonds to form proteins.
proteins: structure ,types and purification techniques
This document provides information on proteins including their structure, types, and purification techniques. It begins with definitions of proteins and amino acids. It then describes the primary, secondary, tertiary, and quaternary levels of protein structure. The document outlines different classifications of amino acids and discusses essential aspects. Finally, it details several common protein purification techniques such as ammonium sulfate precipitation, dialysis, gel filtration chromatography, ion exchange chromatography, and affinity chromatography.
Lecture 1. Proteins.-1.doc
This document provides information on protein structure and functions. It discusses that proteins are polymers made of amino acids and perform many important functions in the body, including structural support, enzymatic reactions, transport, regulation, contraction, storage, and defense. It describes the four levels of protein structure - primary, secondary, tertiary, and quaternary. The document also discusses properties of proteins like solubility and isoelectric point. It explains that denaturation involves loss of structure but not primary sequence, and lists various physical and chemical agents that can cause protein denaturation, such as temperature, pH, organic solvents, and heavy metals.
Proteins
Protein are the most abundant organic molecule of living systems. They occur in every part of the cell and constitutive about 50% of the cellular dry weight.Proteins form the fundamental basis of structure and functional unit of life. Unlike lipids and carbohydrates, proteins are not stored, so they must be consumed daily.
Current recommended daily intake for adults is 0.8 grams of protein per kg of body weight (more is needed for children). Dietary protein comes from eating meat and milk.
Proteins lecture 11
This document discusses the structure of proteins at multiple levels:
1. It describes the primary structure of proteins as the unique sequence of amino acids determined by genes. The peptide bond links amino acids and is rigid and planar.
2. Secondary structures like alpha helices and beta sheets form due to hydrogen bonding between amino acids in close proximity in the sequence. Alpha helices are tightly coiled and stabilized by hydrogen bonds between amino and carbonyl groups.
3. Tertiary structure refers to the compact three-dimensional folding of the protein chain, bringing hydrophobic residues inwards and hydrophilic outwards. Disulfide bonds and other interactions contribute to tertiary structure.
4. Some proteins have quaternary structure
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.
Similar to A QUICK GLANCE AT PROTEIN STRUCTURE (20)
Protein metabolism and nitrogen fixation and metabolism
Protein metabolism and nitrogen fixation and metabolism
Introduction to Proteins and Aminoacids with Clinical significance
Introduction to Proteins and Aminoacids with Clinical significance
proteins: structure ,types and purification techniques
proteins: structure ,types and purification techniques
Recently uploaded
বাংলাদেশ অর্থনৈতিক সমীক্ষা (Economic Review) ২০২৪ UJS App.pdf
বাংলাদেশের অর্থনৈতিক সমীক্ষা ২০২৪ [Bangladesh Economic Review 2024 Bangla.pdf] কম্পিউটার , ট্যাব ও স্মার্ট ফোন ভার্সন সহ সম্পূর্ণ বাংলা ই-বুক বা pdf বই " সুচিপত্র ...বুকমার্ক মেনু 🔖 ও হাইপার লিংক মেনু 📝👆 যুক্ত ..
আমাদের সবার জন্য খুব খুব গুরুত্বপূর্ণ একটি বই ..বিসিএস, ব্যাংক, ইউনিভার্সিটি ভর্তি ও যে কোন প্রতিযোগিতা মূলক পরীক্ষার জন্য এর খুব ইম্পরট্যান্ট একটি বিষয় ...তাছাড়া বাংলাদেশের সাম্প্রতিক যে কোন ডাটা বা তথ্য এই বইতে পাবেন ...
তাই একজন নাগরিক হিসাবে এই তথ্য গুলো আপনার জানা প্রয়োজন ...।
বিসিএস ও ব্যাংক এর লিখিত পরীক্ষা ...+এছাড়া মাধ্যমিক ও উচ্চমাধ্যমিকের স্টুডেন্টদের জন্য অনেক কাজে আসবে ...
How to Create a More Engaging and Human Online Learning Experience
How to Create a More Engaging and Human Online Learning Experience Wahiba Chair Training & Consulting
Wahiba Chair's Talk at the 2024 Learning Ideas Conference. Main Java[All of the Base Concepts}.docx
This is part 1 of my Java Learning Journey. This Contains Custom methods, classes, constructors, packages, multithreading , try- catch block, finally block and more.
Traditional Musical Instruments of Arunachal Pradesh and Uttar Pradesh - RAYH...
Traditional Musical Instruments of Arunachal Pradesh and Uttar Pradesh
ANATOMY AND BIOMECHANICS OF HIP JOINT.pdf
it describes the bony anatomy including the femoral head , acetabulum, labrum . also discusses the capsule , ligaments . muscle that act on the hip joint and the range of motion are outlined. factors affecting hip joint stability and weight transmission through the joint are summarized.
LAND USE LAND COVER AND NDVI OF MIRZAPUR DISTRICT, UP
This Dissertation explores the particular circumstances of Mirzapur, a region located in the
core of India. Mirzapur, with its varied terrains and abundant biodiversity, offers an optimal
environment for investigating the changes in vegetation cover dynamics. Our study utilizes
advanced technologies such as GIS (Geographic Information Systems) and Remote sensing to
analyze the transformations that have taken place over the course of a decade.
The complex relationship between human activities and the environment has been the focus
of extensive research and worry. As the global community grapples with swift urbanization,
population expansion, and economic progress, the effects on natural ecosystems are becoming
more evident. A crucial element of this impact is the alteration of vegetation cover, which plays a
significant role in maintaining the ecological equilibrium of our planet.Land serves as the foundation for all human activities and provides the necessary materials for
these activities. As the most crucial natural resource, its utilization by humans results in different
'Land uses,' which are determined by both human activities and the physical characteristics of the
land.
The utilization of land is impacted by human needs and environmental factors. In countries
like India, rapid population growth and the emphasis on extensive resource exploitation can lead
to significant land degradation, adversely affecting the region's land cover.
Therefore, human intervention has significantly influenced land use patterns over many
centuries, evolving its structure over time and space. In the present era, these changes have
accelerated due to factors such as agriculture and urbanization. Information regarding land use and
cover is essential for various planning and management tasks related to the Earth's surface,
providing crucial environmental data for scientific, resource management, policy purposes, and
diverse human activities.
Accurate understanding of land use and cover is imperative for the development planning
of any area. Consequently, a wide range of professionals, including earth system scientists, land
and water managers, and urban planners, are interested in obtaining data on land use and cover
changes, conversion trends, and other related patterns. The spatial dimensions of land use and
cover support policymakers and scientists in making well-informed decisions, as alterations in
these patterns indicate shifts in economic and social conditions. Monitoring such changes with the
help of Advanced technologies like Remote Sensing and Geographic Information Systems is
crucial for coordinated efforts across different administrative levels. Advanced technologies like
Remote Sensing and Geographic Information Systems
9
Changes in vegetation cover refer to variations in the distribution, composition, and overall
structure of plant communities across different temporal and spatial scales. These changes can
occur natural.
Your Skill Boost Masterclass: Strategies for Effective Upskilling
Your Skill Boost Masterclass: Strategies for Effective UpskillingExcellence Foundation for South Sudan
Strategies for Effective Upskilling is a presentation by Chinwendu Peace in a Your Skill Boost Masterclass organisation by the Excellence Foundation for South Sudan on 08th and 09th June 2024 from 1 PM to 3 PM on each day.How to deliver Powerpoint Presentations.pptx
"How to make and deliver dynamic presentations by making it more interactive to captivate your audience attention"
ISO/IEC 27001, ISO/IEC 42001, and GDPR: Best Practices for Implementation and...
Denis is a dynamic and results-driven Chief Information Officer (CIO) with a distinguished career spanning information systems analysis and technical project management. With a proven track record of spearheading the design and delivery of cutting-edge Information Management solutions, he has consistently elevated business operations, streamlined reporting functions, and maximized process efficiency.
Certified as an ISO/IEC 27001: Information Security Management Systems (ISMS) Lead Implementer, Data Protection Officer, and Cyber Risks Analyst, Denis brings a heightened focus on data security, privacy, and cyber resilience to every endeavor.
His expertise extends across a diverse spectrum of reporting, database, and web development applications, underpinned by an exceptional grasp of data storage and virtualization technologies. His proficiency in application testing, database administration, and data cleansing ensures seamless execution of complex projects.
What sets Denis apart is his comprehensive understanding of Business and Systems Analysis technologies, honed through involvement in all phases of the Software Development Lifecycle (SDLC). From meticulous requirements gathering to precise analysis, innovative design, rigorous development, thorough testing, and successful implementation, he has consistently delivered exceptional results.
Throughout his career, he has taken on multifaceted roles, from leading technical project management teams to owning solutions that drive operational excellence. His conscientious and proactive approach is unwavering, whether he is working independently or collaboratively within a team. His ability to connect with colleagues on a personal level underscores his commitment to fostering a harmonious and productive workplace environment.
Date: May 29, 2024
Tags: Information Security, ISO/IEC 27001, ISO/IEC 42001, Artificial Intelligence, GDPR
-------------------------------------------------------------------------------
Find out more about ISO training and certification services
Training: ISO/IEC 27001 Information Security Management System - EN | PECB
ISO/IEC 42001 Artificial Intelligence Management System - EN | PECB
General Data Protection Regulation (GDPR) - Training Courses - EN | PECB
Webinars: https://pecb.com/webinars
Article: https://pecb.com/article
-------------------------------------------------------------------------------
For more information about PECB:
Website: https://pecb.com/
LinkedIn: https://www.linkedin.com/company/pecb/
Facebook: https://www.facebook.com/PECBInternational/
Slideshare: http://www.slideshare.net/PECBCERTIFICATION
The Diamonds of 2023-2024 in the IGRA collection
A review of the growth of the Israel Genealogy Research Association Database Collection for the last 12 months. Our collection is now passed the 3 million mark and still growing. See which archives have contributed the most. See the different types of records we have, and which years have had records added. You can also see what we have for the future.
How to Make a Field Mandatory in Odoo 17
In Odoo, making a field required can be done through both Python code and XML views. When you set the required attribute to True in Python code, it makes the field required across all views where it's used. Conversely, when you set the required attribute in XML views, it makes the field required only in the context of that particular view.
Wound healing PPT
This document provides an overview of wound healing, its functions, stages, mechanisms, factors affecting it, and complications.
A wound is a break in the integrity of the skin or tissues, which may be associated with disruption of the structure and function.
Healing is the body’s response to injury in an attempt to restore normal structure and functions.
Healing can occur in two ways: Regeneration and Repair
There are 4 phases of wound healing: hemostasis, inflammation, proliferation, and remodeling. This document also describes the mechanism of wound healing. Factors that affect healing include infection, uncontrolled diabetes, poor nutrition, age, anemia, the presence of foreign bodies, etc.
Complications of wound healing like infection, hyperpigmentation of scar, contractures, and keloid formation.
BÀI TẬP BỔ TRỢ TIẾNG ANH 8 CẢ NĂM - GLOBAL SUCCESS - NĂM HỌC 2023-2024 (CÓ FI...
BÀI TẬP BỔ TRỢ TIẾNG ANH 8 CẢ NĂM - GLOBAL SUCCESS - NĂM HỌC 2023-2024 (CÓ FI...Nguyen Thanh Tu Collection
https://app.box.com/s/y977uz6bpd3af4qsebv7r9b7s21935vdPengantar Penggunaan Flutter - Dart programming language1.pptx
Pengantar Penggunaan Flutter - Dart programming language1.pptx
What is Digital Literacy? A guest blog from Andy McLaughlin, University of Ab...
What is Digital Literacy? A guest blog from Andy McLaughlin, University of Aberdeen
Recently uploaded (20)
বাংলাদেশ অর্থনৈতিক সমীক্ষা (Economic Review) ২০২৪ UJS App.pdf
বাংলাদেশ অর্থনৈতিক সমীক্ষা (Economic Review) ২০২৪ UJS App.pdf
How to Create a More Engaging and Human Online Learning Experience
How to Create a More Engaging and Human Online Learning Experience
Traditional Musical Instruments of Arunachal Pradesh and Uttar Pradesh - RAYH...
Traditional Musical Instruments of Arunachal Pradesh and Uttar Pradesh - RAYH...
Digital Artefact 1 - Tiny Home Environmental Design
Digital Artefact 1 - Tiny Home Environmental Design
LAND USE LAND COVER AND NDVI OF MIRZAPUR DISTRICT, UP
LAND USE LAND COVER AND NDVI OF MIRZAPUR DISTRICT, UP
Your Skill Boost Masterclass: Strategies for Effective Upskilling
Your Skill Boost Masterclass: Strategies for Effective Upskilling
ISO/IEC 27001, ISO/IEC 42001, and GDPR: Best Practices for Implementation and...
ISO/IEC 27001, ISO/IEC 42001, and GDPR: Best Practices for Implementation and...
Liberal Approach to the Study of Indian Politics.pdf
Liberal Approach to the Study of Indian Politics.pdf
BÀI TẬP BỔ TRỢ TIẾNG ANH 8 CẢ NĂM - GLOBAL SUCCESS - NĂM HỌC 2023-2024 (CÓ FI...
BÀI TẬP BỔ TRỢ TIẾNG ANH 8 CẢ NĂM - GLOBAL SUCCESS - NĂM HỌC 2023-2024 (CÓ FI...
Pengantar Penggunaan Flutter - Dart programming language1.pptx
Pengantar Penggunaan Flutter - Dart programming language1.pptx
What is Digital Literacy? A guest blog from Andy McLaughlin, University of Ab...
What is Digital Literacy? A guest blog from Andy McLaughlin, University of Ab...
A QUICK GLANCE AT PROTEIN STRUCTURE
- 1. Understanding Protein Structure Gabrielle Roberts Biology Department, Long Island University, Brooklyn, NY
- 5. Chemical Reactions: Enzymes Cell Signaling: Hormones Transport: Red Blood cells Immunity: Antibodies
- 7. Muscle Tissues: Actin and Myosin Hair & Nails: Keratin Cytoskeleton: Microtubules, intermediate filaments, microfilaments Collagen “fibrous protein”: bones, tendons,
- 16. Alpha & Beta: Working Together The green fluorescent protein : Composed of Beta pleated sheets (in yellow) which forms the outside structure of the protein and an alpha helix structure in the interior of the protein (in purple ).
- 21. Quaternary Protein: Antibody Light chain & Heavy Chain connected by di-sulfide bonds