CRYSTALLOGRAPHIC STUDIES OF THE DYNAMIC PROPERTIES OF LYSOZYME

被引:410
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
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.
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页码:563 / 568
页数:6
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