Protein’s primary, secondary, tertiary, quarternary structure

Proteins structures are made by condensation of amino acids forming peptide bonds. The sequence of amino acids in a protein is called its primary structure. The secondary structure is determined by the dihedral angles of the peptide bonds, the tertiary structure by the folding of proteins chains in space. Association of folded polypeptide molecules to complex functional proteins results in quaternary structure. Levels of Protein Structure 1. Primary Structure of Protein The Primary structure of proteins is the exact ordering of amino acids forming their chains. The exact sequence of the proteins is very important as it determines the final fold and therefore the function of the protein. The number of polypeptide chains together form proteins. These chains have amino acids arranged in a particular sequence which is characteristic of the specific protein. Any change in the sequence changes the entire protein. The following picture represents the primary protein structure (an amino acid chain). As you might expect, the amino acid sequence within the polypeptide chain is crucial for the protein’s proper functioning. This sequence is encrypted in the DNA genetic code. If mutation is present in the DNA and the amino acid sequence is changed, the protein function may be affected. The protein ‘s primary structure is the amino acid sequence in its polypeptide chain. If proteins were popcorn stringers designed to decorate a Christmas tree, a protein ‘s primary structure is the sequence in which various shapes and varieties of popped maize are strung together. Covalent, peptide bonds which connect the amino acids together maintain the primary structure of a protein. The following figure shows the primary insulin structure, which is the first protein to be sequenced. Notice the position of each amino acid numerated on the right side of the figure. By convention, biochemists often list the amino acids that begin at the polypeptide chain’s amino-terminus. All documented genetic disorders, such as cystic fibrosis, sickle cell anemia, albinism, etc., are caused by mutations resulting in alterations in the primary protein structures, which in turn lead to alterations in the secondary , tertiary and probably quarterly structure. Amino acids are small organic molecules consisting of a chiral carbon with four substituents. Of those only the fourth the side chain is different among amino acids. 2. Secondary Structure of Protein The proteins do not exist in just simple chains of polypeptides. These polypeptide chains usually fold due to the interaction between the amine and carboxyl group of the peptide link. The structure refers to the shape in which a long polypeptide chain can exist. They are found to exist in two different types of structures α – helix and β – pleated sheet structures. This structure arises due to the regular folding of the backbone of the polypeptide chain due to hydrogen bonding between -CO group and -NH groups of the peptide bond. However, segments of the protein chain may acquire their own local fold, which is much simpler and usually takes the shape of a spiral an extended shape or a loop. These local folds are termed secondary elements and form the proteins secondary structure. (a) α – Helix: α – Helix is one of the most common ways in which a polypeptide chain forms all possible hydrogen bonds by twisting into a right-handed screw with the -NH group of each amino acid residue hydrogen-bonded to the -CO of the adjacent turn of the helix. The polypeptide chains twisted into a right-handed screw. (b) β – pleated sheet: In this arrangement, the polypeptide chains are stretched out beside one another and then bonded by intermolecular H-bonds. In this structure, all peptide chains are stretched out to nearly maximum extension and then laid side by side which is held together by intermolecular hydrogen bonds. The structure resembles the pleated folds of drapery and therefore is known as β – pleated sheet 3. Tertiary Structure of Protein This structure arises from further folding of the secondary structure of the protein. H-bonds, electrostatic forces, disulphide linkages, and Vander Waals forces stabilize this structure. The tertiary structure of proteins represents overall folding of the polypeptide chains, further folding of the secondary structure. It gives rise to two major molecular shapes called fibrous and globular. The main forces which stabilize the secondary and tertiary structures of proteins are hydrogen bonds, disulphide linkages, van der Waals and electrostatic forces of attraction. 4. Quaternary Structure of Protein The spatial arrangement of various tertiary structures gives rise to the quaternary structure. Some of the proteins are composed of two or more polypeptide chains referred to as sub-units. The spatial arrangement of these subunits with respect to each other is known as quaternary structure. #proteins #aminoAcids #peptides #globularProteins #fibrousProteins #NikolaysGenetics