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Extended conformations of polypeptides and proteins in urea and guanidine hydrochloride
Author(s) -
Tiffany M. Lois,
Krimm S.
Publication year - 1973
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1973.360120310
Subject(s) - guanidine , chemistry , hydrochloride , random coil , urea , circular dichroism , hydrogen bond , denaturation (fissile materials) , crystallography , stereochemistry , molecule , organic chemistry , nuclear chemistry
By analyzing the effect of urea and guanidine hydrochloride on the circular dichroism of many polypeptides and proteins, it is concluded that under conditions of high concentration of the perturbant and at low temperatures the resultant state approached is that of a local extended helix structure instead of a completely random coil. Intensification by urea and guanidine hydrochloride of the circular dichroism bands of poly‐ L ‐proline II leads to the proof that the mechanism of interaction of urea and guanidine hydrochloride with proteins is through hydrogen bonding to the backbone carbonyl group.