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Transmission of conformational change in insulin Cyrus Chothia*†, Arthur M. Lesk* , Guy G. Dodson‡ & Dorothy C. Hodgkin§
*Medical Research Council, Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
†William Ramsay, Ralph Foster and Christopher Ingold Laboratories, University College London, Gower Street, London WC1E 6BT, UK
‡Department of Chemistry, University of York, Heslington, York YO1 5DD, UK
§Chemical Crystallography Laboratory, Parks Road, Oxford OX1 3PD, UK
Permanent address: Fairleigh Dickinson University, Teaneck-Hackensack Campus, Teaneck, New Jersey 07666, USA.
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 Å. This limits the extent to which conformational changes can be dissipated locally, causing their transmission over long distances.
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