MEASUREMENT OF THERMODYNAMIC NONIDEALITY ARISING FROM VOLUME-EXCLUSION INTERACTIONS BETWEEN PROTEINS AND POLYMERS

被引：32

作者：

WILLS, PR

GEORGALIS, Y

DIJK, J

WINZOR, DJ

机构：

[1] FREE UNIV BERLIN,INST KRISTALLOG,BERLIN 33,GERMANY

[2] LEIDEN UNIV,SYLVIUS LAB,DEPT BIOCHEM MED,2300 RA LEIDEN,NETHERLANDS

[3] UNIV QUEENSLAND,DEPT BIOCHEM,CTR PROT STRUCT FUNCT & ENGN,BRISBANE,QLD 4072,AUSTRALIA

来源：

BIOPHYSICAL CHEMISTRY | 1995年 / 57卷 / 01期

基金：

澳大利亚研究理事会;

关键词：

EXCLUDED VOLUME; MOLECULAR CROWDING; PROTEIN POLYMER INTERACTIONS; 2ND VIRIAL COEFFICIENTS; THERMODYNAMIC NONIDEALITY;

D O I：

10.1016/0301-4622(95)00043-W

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 effective thermodynamic radii of 23 ribosomal proteins from the 50 S subunit have been determined by gel chromatography on Sephadex G-50, thereby supporting the contention that most of the proteins of the 50 S ribosomal unit exhibit reasonably globular structures. To investigate further the usefulness of modelling proteins as spheres, the second virial coefficient describing excluded volume interactions of some ribosomal proteins with two inert polymers, polyethylene glycol (PEG) and dextran, has been determined by gel chromatography and/or sedimentation equilibrium techniques. Protein-polymer excluded volumes obtained with PEG 20000 and Dextran T70 as the space-filling solute are shown to conform reasonably well with a quantitative expression describing interaction between an impenetrable sphere and an ideal Brownian path (K.M. Jansons and C.G. Phillips, J. Colloid Interface Sci., 137 (1990) 75).

引用

页码：37 / 46

页数：10

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