CORRELATED INTRAMOLECULAR MOTIONS AND DIFFUSE-X-RAY SCATTERING IN LYSOZYME

被引：60

作者：

FAURE, P

MICU, A

PERAHIA, D

DOUCET, J

SMITH, JC

BENOIT, JP

机构：

[1] CEA SACLAY,DBCM,BIOPHYS PROT & MEMBRANES SECT,F-91191 GIF SUR YVETTE,FRANCE

[2] UNIV PARIS 11,CNRS,ENZYMOL PHYSICOCHIM & MOLEC LAB,RECH GRP,F-91405 ORSAY,FRANCE

[3] UNIV PARIS 11,PHYS SOLIDE LAB,F-91405 ORSAY,FRANCE

来源：

NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 02期

关键词：

D O I：

10.1038/nsb0294-124

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：

Correlated motions of protein atoms ave of biological significance in processes involving ligand binding, conformational change and information transmission. X-ray scattering patterns from protein crystals contain diffuse scattering that originates from correlated displacements of atoms. Here we present experimental data on diffuse X-ray scattering from lysozyme crystals. We show that the diffuse scattering is similar in form to scattering derived from molecular dynamics simulation and normal mode analysis of the isolated protein, the normal modes giving the closest agreement with experiment.

引用

页码：124 / 128

页数：5

共 28 条

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