Transmission of conformational change in insulin

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

doi:10.1038/302500a0

Transmission of conformational change in insulin

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

Biochemistry & Molecular Biology

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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 language	English (US)
Pages (from-to)	500-505
Number of pages	6
Journal	Nature
Volume	302
Issue number	5908
DOIs	https://doi.org/10.1038/302500a0
State	Published - 1983

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title = "Transmission of conformational change in insulin",

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.",

author = "Cyrus Chothia and Lesk, {Arthur M.} and Dodson, {Guy G.} and Hodgkin, {Dorothy C.}",

year = "1983",

doi = "10.1038/302500a0",

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journal = "Nature",

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T1 - Transmission of conformational change in insulin

AU - Chothia, Cyrus

AU - Lesk, Arthur M.

AU - Dodson, Guy G.

AU - Hodgkin, Dorothy C.

PY - 1983

Y1 - 1983

N2 - 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.

AB - 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.

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U2 - 10.1038/302500a0

DO - 10.1038/302500a0

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VL - 302

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JO - Nature

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ER -

Transmission of conformational change in insulin

Abstract

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