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Literature DB >> 460438

Crystallographic studies of the dynamic properties of lysozyme.

P J Artymiuk, C C Blake, D E Grace, S J Oatley, D C Phillips, M J Sternberg.

Abstract

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.

Entities: Gene Species

Mesh：

Substances：
Muramidase

Year: 1979 PMID： 460438 DOI： 10.1038/280563a0

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

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Cited

61 in total

Crystallographic studies of the dynamic properties of lysozyme.

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