Proteins exhibit two secondary structures, a-helix, and b-pleated sheet, resulting from hydrogen bonding between >C=O and –NH– groups in the peptide bond. The a-helix forms a right-handed screw, while the b-pleated sheet resembles pleated folds of drapery.
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The two types of secondary structures in proteins are α-helices and β-sheets. In α-helices, the polypeptide chain forms a helical coil stabilized by intramolecular hydrogen bonds between the amino and carboxyl groups of nearby residues. β-sheets involve the alignment of polypeptide strands, forming a sheet-like structure stabilized by hydrogen bonds between adjacent strands. Hydrogen bonding plays a crucial role in maintaining the structural stability of both secondary structures, contributing to the unique three-dimensional folding of proteins. This bonding pattern influences the overall shape and function of proteins in biological systems.