Primary structure of proteins
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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.
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The document discusses the levels of protein structure from primary to quaternary structure. It defines the primary structure as the amino acid sequence. Secondary structure forms from hydrogen bonding between amino acids and includes alpha helices and beta pleated sheets. Tertiary structure results from folding influenced by interactions between amino acid side chains. Quaternary structure occurs when multiple polypeptide chains interact to form a protein complex. Examples including hemoglobin and glyceraldehyde-3-phosphate dehydrogenase are provided to illustrate the different levels of structure.
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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.
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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.
Quaternary structure of protein
Quaternary structure refers to the arrangement of multiple protein subunits into a single protein complex. Hemoglobin is a common example that is made of two alpha and two beta subunits. The subunits interact through hydrophobic interactions, hydrogen bonding, and other bonds. Globular proteins tend to have quaternary structure that clusters the subunits into a spherical shape, while fibrous proteins form long coils or sheets through interactions between subunits. Quaternary structure allows proteins to take on specialized functions beyond what individual subunits could achieve alone.
Secondary Structure Prediction of proteins
Secondary structure prediction has been around for almost a quarter of a century. The early methods suffered from a lack of data. Predictions were performed on single sequences rather than families of homologous sequences, and there were relatively few known 3D structures from which to derive parameters. Probably the most famous early methods are those of Chou & Fasman, Garnier, Osguthorbe & Robson (GOR) and Lim. Although the authors originally claimed quite high accuracies (70-80 %), under careful examination, the methods were shown to be only between 56 and 60% accurate (see Kabsch & Sander, 1984 given below). An early problem in secondary structure prediction had been the inclusion of structures used to derive parameters in the set of structures used to assess the accuracy of the method.
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Protein structure and function are described, including primary, secondary, tertiary, and quaternary structure. Hemoglobin and myoglobin are discussed as examples of heme proteins that transport oxygen. Hemoglobin has a cooperative binding curve due to its allosteric nature, allowing it to efficiently bind and release oxygen in the lungs and tissues. The binding of oxygen causes a conformational change in hemoglobin subunits from the tense T state to relaxed R state, facilitating additional oxygen binding in a cooperative manner.
Chapter 3(part1) - Amino acids, peptides, and proteins
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Water activity
Water activity is the moisture content of the food which is available for microbial growth.By controlling water activity the food can be preserved for longer duration
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Chapter 3(part1) - Amino acids, peptides, and proteins
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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.
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.
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Primary structure of proteins
- 1. Protein structure Organizational level
- 2. • The structure of the protein molecule includes four organizational levels. • 1) primary • 2)secondary • 3)tertiary • 4)quaternary
- 3. Primary structure • Primary structure of protein is defined as • the sequence of amino acids . • Importance: • 1)detection of genetic diseases • 2)Improper folding • 3)loss or impairment of normal function
- 4. Peptide bond • The peptide bonds are amide linkages • Between two amino acids in which the • Alpha carboxyl group of one amino acid is attached to the alpha amino group of the other amino acid. • Example..valine and alanine form dipeptide valylalanine.
- 5. Breaking of peptide bond • Unlike proteins which are denatured by conditions such as : • 1)Heating • 2)High concentration of urea • Peptides are broken by :prolonged exposure to : • Strong acid or base at elevated temperature.This hydrolyzes these bonds non-enzymically.