Crystallographic studies of the dynamic properties of lysozyme View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1979-08

AUTHORS

P. J. Artymiuk, C. C. F. Blake, D. E. P. Grace, S. J. Oatley, D. C. Phillips, M. J. E. 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. More... »

PAGES

563-568

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/280563a0

DOI

http://dx.doi.org/10.1038/280563a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016219835

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/460438


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