Protein hydration in solution: Experimental observation by x-ray and neutron scattering

被引：801

作者：

Svergun, DI

Richard, S

Koch, MHJ

Sayers, Z

Kuprin, S

Zaccai, G

机构：

[1] DESY, European Mol Biol Lab, Hamburg Outstn, D-22603 Hamburg, Germany

[2] Russian Acad Sci, Inst Crystallog, Moscow 117333, Russia

[3] Inst Biol Struct, F-38027 Grenoble 1, France

[4] Karolinska Inst, Med Nobel Inst Bioichem, S-17177 Stockholm, Sweden

[5] Inst Max Von Laue Paul Langevin, F-38042 Grenoble 9, France

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1998年 / 95卷 / 05期

关键词：

D O I：

10.1073/pnas.95.5.2267

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 structure of the protein-solvent interface is the subject of controversy in theoretical studies and requires direct experimental characterization. Three proteins with known atomic resolution crystal structure (lysozyme, Escherichia coli thioredoxin reductase, and protein R1 of E. coli ribonucleotide reductase) were investigated in parallel by x-ray and neutron scattering in H2O and D2O solutions. The analysis of the protein-solvent interface is based on the significantly different contrasts for the protein and for the hydration shell. The results point to the existence of a first hydration shell with an average density approximate to 10% larger than that of the bulk solvent in the conditions studied. Comparisons with the results of other studies suggest that this may be a general property of aqueous interfaces.

引用

页码：2267 / 2272

页数：6

共 49 条

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