CRYSTALLOGRAPHIC STUDIES OF THE DYNAMIC PROPERTIES OF LYSOZYME

被引：409

作者：

ARTYMIUK, PJ ^{[1
]}

BLAKE, CCF ^{[1
]}

GRACE, DEP ^{[1
]}

OATLEY, SJ ^{[1
]}

PHILLIPS, DC ^{[1
]}

STERNBERG, MJE ^{[1
]}

机构：

[1] ZOOL DEPT,MOLEC BIOPHYS LAB,S PARKS RD,OXFORD,ENGLAND

来源：

NATURE | 1979年 / 280卷 / 5723期

关键词：

D O I：

10.1038/280563a0

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 patterns of atomic displacements in the crystals of hen and human lysozyme derived from independent crystallographic refinement are broadly similar. Analysis of the pattern indicates a close correlation with molecular structure, strongly suggestive of intramolecular motion. The active site of lysozyme is located in a region of high displacement. It is concluded that protein mobility may play a significant part in biological activity and that X-ray crystallography can contribute to its analysis. © 1979 Nature Publishing Group.

引用

页码：563 / 568

页数：6

共 35 条

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