PMID: 1544477Mar 24, 1992

Biphasic transition curve on denaturation of chicken cystatin by guanidinium chloride. Evidence for an independently unfolding structural region

FEBS Letters
I Björk, E Pol

Abstract

Far-ultraviolet circular dichroism and tryptophan fluorescence measurements showed that the reversible unfolding of the cysteine proteinase inhibitor, chicken cystatin, by guanidinium chloride is a two-step process with transition midpoints at approximately 3.4 and approximately 5.4 M denaturant. The partially unfolded intermediate had both far- and near-ultraviolet circular dichroism and fluorescence emission spectra comparable to those of the native protein. The largely retained tertiary structure suggests that the intermediate represents a species in which a separate region of lower stability has been unfolded, rather than an intermediate of the 'molten globule' type. Such a structurally independent region is apparent in the three-dimensional structure of the inhibitor.

References

Jan 1, 1990·Annual Review of Biochemistry·P S Kim, R L Baldwin
Feb 21, 1989·Biochemistry·I BjörkK Ylinenjärvi
Jan 1, 1973·International Journal of Peptide and Protein Research·M CortijoW B Gratzer
Feb 1, 1984·The Biochemical Journal·C SchwabeA J Barrett
Dec 28, 1964·Annals of the New York Academy of Sciences·B J DAVIS

Related Concepts

Circular Dichroism, Vibrational
Guanidines
Protein Conformation
Protein Denaturation
Fluorescence Spectroscopy
Cystatin-Related Proteins
Guanidine Sulfite (1: 1)

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