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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Chothia, C., Lesk, A., Dodson, G. et al. Transmission of conformational change in insulin. Nature 302, 500–505 (1983). https://doi.org/10.1038/302500a0
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DOI: https://doi.org/10.1038/302500a0
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