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Transmission of conformational change in insulin

Naturevolume 302pages500505 (1983) | Download Citation

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

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Affiliations

  1. Medical Research Council, Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    • Cyrus Chothia
    •  & Arthur M. Lesk
  2. William Ramsay, Ralph Foster and Christopher Ingold Laboratories, University College London, Gower Street, London, WC1E 6BT, UK

    • Cyrus Chothia
  3. Department of Chemistry, University of York, Heslington, York, YO1 5DD, UK

    • Guy G. Dodson
  4. Chemical Crystallography Laboratory, Parks Road, Oxford, OX1 3PD, UK

    • Dorothy C. Hodgkin
  5. Fairleigh Dickinson University, Teaneck-Hackensack Campus, Teaneck, New Jersey, 07666, USA

    • Arthur M. Lesk

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https://doi.org/10.1038/302500a0

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