Abstract
Serum albumin is known to act as a carrier for a variety of molecules and metal ions. This property of the protein could be due to the presence of different types of secondary structures in its molecules. The most commonly known are the α-helix, β-sheets, β-turns and random coil forms. A rigorous analysis of human serum albumin has been carried out by using four different approaches. Comparative studies have revealed that the segment Asp 107 to Val 122 of this protein assumes a γ-helical structure. Under favourable circumstances, two prolines at the i and ( i + 5) th positions can initiate a γ-helix. Further requirements for the formation and stability of γ-helix are discussed.
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