Keywords

Peptides, Secondary Structure, Hydration, Infrared Spectroscopy

Abstract

Polylysine (PLys, MW14000), polylysine hydrogen bromide conjugate (PLvs-HBr, MW55000) and polysodium glutamate (PGA- The secondary structure of Na, MW80000) changes with time. At RH=60%, the three polypeptides transform from random coil to ¦Â-structure in a similar time, which takes about 9 minutes; while the transformation from ¦Á-to ¦Â-structure When , the time required for PGA-Na is about twice that of PLas and PLys-HBr. However, when RH=90%, when the ¦Â-to ¦Á-structure transforms, the time required for PLys and PLys-HBr is reversed to that of PGA- Twice that of Na. When transforming from random coil to ¦Á-structure at about RH=90%, PLys and PLys-HBr appear ¦Â-sheet structures, while PGA-Na does not. Experiments show that under different hydration degrees Effect of chain groups on conformational changes.

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Original research done by Yang Jingwen, Zhang Jizhen, Niu Zeling

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