| Literature DB >> 6339948 |
C Chothia, A M Lesk, G G Dodson, D C Hodgkin.
Abstract
Crystal structures of insulin contain molecules that are similar but not identical in conformation. Packed helices move relative to each other, these shifts being accommodated by motions of side-chain atoms arising from small changes in torsion angles. Such low-energy conformational adjustments can accommodate shifts of no more than approximately 1.5 A. This limits the extent to which conformational changes can be dissipated locally, causing their transmission over long distances.Entities:
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Year: 1983 PMID： 6339948 DOI： 10.1038/302500a0
Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962