Transmission of conformational change in insulin

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

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