SOLVENT DEPENDENCE OF DIMENSIONS OF UNFOLDED PROTEIN CHAINS

被引：18

作者：

DAMASCHUN, G ^{[1
]}

DAMASCHUN, H ^{[1
]}

GAST, K ^{[1
]}

ZIRWER, D ^{[1
]}

BYCHKOVA, VE ^{[1
]}

机构：

[1] ACAD SCI USSR,INST PROTEIN RES,PUSHCHINO 142292,USSR

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 1991年 / 13卷 / 04期

关键词：

PROTEIN; DENATURATION; UNFOLDED PROTEINS; SMALL-ANGLE X-RAY SCATTERING; DYNAMIC LIGHT SCATTERING; CYTOCHROME-C;

D O I：

10.1016/0141-8130(91)90062-Y

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：

The radii of gyration of unfolded apo-cytochrome C at pH 2.3 have been determined in three conditions: (i) 20 mM sodium phosphate buffer; (ii) 0.25 M NaCl; and (iii) 6.65 M GuHCl by small-angle X-ray scattering, and (iii) from translational diffusion coefficients measured by dynamic light scattering. The radius of gyration of the unfolded protein chain depends remarkably on the quality of the solvent, decreasing in the order 20 mM sodium phosphate > 6.65 M GuHCl > 0.25 M NaCl. The value of the radius of gyration in 0.25 M NaCl and also the value estimated for infinite ionic strength are close to the value predicted theoretically for the theta-point. This means that water in the absence of electrostatic interactions is a poor solvent for an unfolded protein while 6.65 M GuHCl is a better solvent.

引用

页码：217 / 221

页数：5

共 27 条

[11] SPECIFIC INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINS AND THE MECHANISM OF PROTEIN FOLDING [J].