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 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. 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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