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Conformational changes of pinellin in solution using intrinsic fluorescence and CD as probes
Author(s) -
Lu ZiXian,
Shi QingLuo,
Xu QingYu
Publication year - 1986
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.360250303
Subject(s) - chemistry , fluorescence , guanidine , biophysics , denaturation (fissile materials) , side chain , hydrochloride , native state , crystallography , stereochemistry , biochemistry , polymer , organic chemistry , quantum mechanics , nuclear chemistry , biology , physics
Pinellin is a plant protein extracted from the rhizome of the Chinese herb Pinellia . It has the ability to abort early pregnancy in mice as well as in rabbits. Studies on the conformational changes of pinellin have been carried out in our laboratory using intrinsic fluorescence and CD. Experimental results show that some tryptophanyl side chains are buried more deeply than others, which results in the heterogeneity of tryptophanyl emission. CD data indicated a high content of β‐pleated sheet and β‐turn for the backbone conformation. The results of fluorescence and CD measurements both demonstrated the presence of intermediates along the path of denaturation. The following was proposed as the unfolding mechanism of pinellin in 6 M guanidine hydrochloride: native state → first intermediate → second intermediate → fully unfolded state.