ACID-INDUCED FOLDING OF PROTEINS

被引：601

作者：

GOTO, Y ^{[1
]}

CALCIANO, LJ ^{[1
]}

FINK, AL ^{[1
]}

机构：

[1] UNIV CALIF SANTA CRUZ,DEPT CHEM,SANTA CRUZ,CA 95064

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1990年 / 87卷 / 02期

关键词：

Acid denaturation; Anion binding; Molten globule; Protein folding;

D O I：

10.1073/pnas.87.2.573

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The addition of HCl, at low ionic strength, to the native state of apomyoglobin, β-lactamase, and cytochrome c caused these proteins to adopt an essentially fully unfolded conformation in the vicinity of pH 2. However, contrary to expectation, the addition of further acid resulted in refolding to a compact conformation with the properties of a molten globule. The major factor responsible for the refolding is believed to be the binding of the anion, which minimizes the intramolecular charge repulsion that initially brought about the unfolding.

引用

页码：573 / 577

页数：5

共 16 条

[1] ACID UNFOLDING AND SELF-ASSOCIATION OF RECOMBINANT ESCHERICHIA-COLI DERIVED HUMAN INTERFERON-GAMMA [J].