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Primary structure of protein Secondary structure of protein Tertiary structure of protein Quaternary structure of protein Methods to determine protein structure Conclusion References METHODS TO DETERMINE PROTEIN STRUCTURE Each protein has a unique sequence of amino acids. The amino acids are held together in a protein by covalent peptide bonds or linkages. A peptide bond are formed when amino group of an amino acid combines with the carboxyl group of another. The conformation of polypeptide chain by twisting or folding is referred to as secondary structure. Two types of secondary structures α-helix and β-sheet are mainly identified. α-Helical structure was proposed by Pauling and Corey in 1951. It occurs when the sequence of amino acids are linked by hydrogen bonds. Each turn of α-helix contains 3.6 amino acids. β-pleated sheets are composed of two or more segments of fully extended peptide chains. β-Sheets may be arranged either in parallel or anti-parallel direction. Many globular proteins contain combinations of α-helix and β-pleated sheet secondary structure, these patterns are called supersecondary structures also called motifs. The three dimensional arrangement of protein structure is referred to as tertiary structure. It is a compact structure with hydrophobic side chains held interior while the hydrophilic groups are on the surface. This type of arrangement provide stability of the molecule. Besides the H-bongs, disulfide bonds, ionic interactions, hydrophobic interactions also contribute to the tertiary structure. STRUCTURAL ORGANIZATION OF PROTEINS

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Proteins are polypeptide structures made up of one or more extended chains of residues from the amino acid. They provide a wide range of organism tasks, including as DNA replication, molecule transport, metabolic process catalysis, and cell structural support. The albumins seen in vast quantities in egg whites typically have a distinct 3D structure as a result of bonds that form between the protein’s various amino acids. These bonds are broken by heating, exposing the hydrophobic (water-hating) amino acids that are typically maintained on the inside of the protein 1, 1 comma, 2 end superscript, 2, start superscript. In an effort to escape the water that surrounds them in the egg white, the hydrophobic amino acids will bind to one another, creating a protein network that gives the egg white structure and makes it white and opaque. Ta-da! Protein denaturation, thank you for another wonderful breakfast Proteins.pdf

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