NMR ANALYSIS OF STAPHYLOCOCCAL NUCLEASE THERMAL QUENCH REFOLDING KINETICS

被引：24

作者：

KAUTZ, RA

FOX, RO

机构：

[1] YALE UNIV,DEPT MOLEC BIOPHYS & BIOCHEM,260 WHITNEY AVE,NEW HAVEN,CT 06511

[2] YALE UNIV,HOWARD HUGHES MED INST,NEW HAVEN,CT 06511

来源：

PROTEIN SCIENCE | 1993年 / 2卷 / 05期

关键词：

NMR; PROLINE ISOMERIZATION; PROTEIN FOLDING; REFOLDING PHASES; STAPHYLOCOCCAL NUCLEASE;

D O I：

10.1002/pro.5560020514

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：

Thermally unfolded staphylococcal nuclease has been rapidly quenched to temperatures near 0-degrees-C and the refolding behavior examined using an NMR kinetic experiment. Unfolded protein, exhibiting random coil chemical shifts, persists following the quench and refolds in two distinct kinetic phases. A protein folding intermediate with a trans Lys 116-Pro 117 peptide bond is transiently overpopulated and relaxes to the predominantly cis native cis-trans equilibrium. The rate of trans --> cis isomerization in the nativelike nuclease intermediate is approximately 100-fold faster than that observed in a Lys-Pro model peptide. The activation enthalpy of 20 kcal/mol observed for the nuclease Lys 116-Pro 117 peptide bond is comparable to that observed for other X-Pro isomerizations.

引用

页码：851 / 858

页数：8

共 36 条

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