Transmission of conformational change in insulin

Cyrus Chothia, Arthur M. Lesk, Guy G. Dodson, Dorothy C. Hodgkin

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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 ∼1.5 . This limits the extent to which conformational changes can be dissipated locally, causing their transmission over long distances.

Original languageEnglish (US)
Pages (from-to)500-505
Number of pages6
JournalNature
Volume302
Issue number5908
DOIs
StatePublished - Dec 1 1983

All Science Journal Classification (ASJC) codes

  • General

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    Chothia, C., Lesk, A. M., Dodson, G. G., & Hodgkin, D. C. (1983). Transmission of conformational change in insulin. Nature, 302(5908), 500-505. https://doi.org/10.1038/302500a0