Peptide bonds, hydrogen bonds, disulfide linkages, van der Waals, and electrostatic forces of attraction are the chemical bonds that stabilize the different structures in primary, secondary, tertiary, and quaternary structures.
The advanced structure of proteins gives rise to two kinds of major molecular shapes which are fibrous as well as globular structures. The main forces which are involved in stabilizing the secondary along with the tertiary structures of proteins include hydrogen bonds, disulfide type linkages, van der Waals attraction, and electrostatic forces of attraction.
The primary structure is generally determined by adjoining peptide bonds where the link is adjoining amino acids in sequential order. Tertiary structure is determined by the existence of disulfide bonds in between hydrophobic interactions as well as cysteine residues whereas the quaternary type structure is determined by multiple subunits of a protein that undergo various interactions.
Hydrogen bonds exist in a protein molecule as its large number can form between adjacent regions of the polypeptide chain in folded form and stabilize its three-dimensional kind of shape.
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