Schematically represent primary, secondary and tertiary structures of a hypothetical polymer say for example a protein.
Schematically represent primary, secondary and tertiary structures of a hypothetical polymer say for example a protein.
Proteins are the large-sized, heteropolymeric macromolecules having on or more polypeptides (chains of amino acid).
Primary structure The primary structure of a protein is the linear sequence of amino acid structural units and partially comprises its overall biomolecular structures. The amino acids are linked together in a sequence by peptide bonds.
Secondary structure It is a three dimensional form of local segments of bipolymers such as proteins. Secondary struture of proteins is defined by hydrogen bonds between backbone amino and carboxyl groups. Mainly secondary structure in proteins possess two forms, i.e., α-helix and β-pleated sheet.
α-helix is a polypeptide chain spirally coiled to form a righ handed helix. This helix may be coiled regularly at places and at some places randomly coiled. The helix is stabilised by many hydrogen bonds which are formed between - CO of one anino acid and - NH group of next fourth amono acid.
β- Pleated sheets two or more polypeptide chains are joined together by intermolecular hydrogen bonds to produce a sheet like structure instead of fibre as in α-helix.The polypeptide strands in a sheet may run parallel in same direction, e.g., keratin or in opposite direction called antiparalel β-sheet, e.g., fibroin.
Tertiary structure involves interactions that are caused by the bending and folding of α-helix orβ-sheets leading to the formation of rods, spheres of fibres. Such interactions are typically corferred by H-bonds, ionic bonds, covalent bonds. van der Waat's interactions and hydrophobic interactions or disulphide linkages. It gives the protein a three dimensional conformation.
Proteins are the large-sized, heteropolymeric macromolecules having on or more polypeptides (chains of amino acid).
Primary structure The primary structure of a protein is the linear sequence of amino acid structural units and partially comprises its overall biomolecular structures. The amino acids are linked together in a sequence by peptide bonds.
Secondary structure It is a three dimensional form of local segments of bipolymers such as proteins. Secondary struture of proteins is defined by hydrogen bonds between backbone amino and carboxyl groups. Mainly secondary structure in proteins possess two forms, i.e., α-helix and β-pleated sheet.
α-helix is a polypeptide chain spirally coiled to form a righ handed helix. This helix may be coiled regularly at places and at some places randomly coiled. The helix is stabilised by many hydrogen bonds which are formed between - CO of one anino acid and - NH group of next fourth amono acid.
β- Pleated sheets two or more polypeptide chains are joined together by intermolecular hydrogen bonds to produce a sheet like structure instead of fibre as in α-helix.The polypeptide strands in a sheet may run parallel in same direction, e.g., keratin or in opposite direction called antiparalel β-sheet, e.g., fibroin.
Tertiary structure involves interactions that are caused by the bending and folding of α-helix orβ-sheets leading to the formation of rods, spheres of fibres. Such interactions are typically corferred by H-bonds, ionic bonds, covalent bonds. van der Waat's interactions and hydrophobic interactions or disulphide linkages. It gives the protein a three dimensional conformation.
