TEMPERATURE-DEPENDENT X-RAY-DIFFRACTION AS A PROBE OF PROTEIN STRUCTURAL DYNAMICS

被引：1070

作者：

FRAUENFELDER, H ^{[1
]}

PETSKO, GA ^{[1
]}

TSERNOGLOU, D ^{[1
]}

机构：

[1] WAYNE STATE UNIV,SCH MED,DEPT BIOCHEM,DETROIT,MI 48201

来源：

NATURE | 1979年 / 280卷 / 5723期

关键词：

D O I：

10.1038/280558a0

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：

X-ray diffraction at four temperatures from 220 to 300 K coupled with crystallographic refinement yields the mean-square displacements and conformational potentials of all 1,261 non-hydrogen atoms of metmyoglobin. The results are interpreted to indicate a condensed core around the haem, semi-liquid regions towards the outside and a possible pathway for ligands. It is concluded that X-ray diffraction can provide the spatial distribution of the dynamic features of a protein. © 1979 Nature Publishing Group.

引用

页码：558 / 563

页数：6

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