The role of Pro20 in the isomerization of myotoxin a from Crotalus viridis viridis:: Folding and structural characterization of synthetic myotoxin a and its Pro20Gly homolog

被引：6

作者：

Nedelkov, D ^{[1
]}

O'Keefe, MP ^{[1
]}

Chapman, TL ^{[1
]}

Bieber, AL ^{[1
]}

机构：

[1] Arizona State Univ, Dept Chem & Biochem, Tempe, AZ 85287 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1997年 / 241卷 / 02期

关键词：

D O I：

10.1006/bbrc.1997.7845

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Biochemical characterization has established the presence of two conformational forms of myotoxin a. To test the hypothesis that this may be due to cis-trans isomerization at Pro20, synthetic versions of myotoxin a and its Pro20-->Gly structural homolog were folded, then purified using a two-step cation-exchange/reverse-phase perfusion chromatography method. The disulfide bond configuration for the folded proteins was found to be the same as that of native myotoxin a CE and RP-HPLC revealed that folded synthetic myotoxin a exists in two conformations while the Pro20-->Gly homolog exists in only one, supporting the hypothesis that cis-trans isomerization at Pro20 is the source of the myotoxin a conformational heterogeneity. (C) 1997 Academic Press.

引用

页码：525 / 529

页数：5

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