Helix movements in proteins

Cyrus Chothia; Arthur M. Lesk

doi:10.1016/0968-0004(85)90270-1

Helix movements in proteins

Cyrus Chothia, Arthur M. Lesk

Biochemistry & Molecular Biology

Research output: Contribution to journal › Review article › peer-review

69 Scopus citations

Abstract

Close-packed α-helices in proteins can move relative to each other by up to ∼1.5 Å by small conformational adjustments in the side-chains that form the interface between them. Such relative helix motions facilitate the long-range transmission of conformational change, examples of which are the closure of clefts between domains in enzymes, and allosteric transitions.

Original language	English (US)
Pages (from-to)	116-118
Number of pages	3
Journal	Trends in Biochemical Sciences
Volume	10
Issue number	3
DOIs	https://doi.org/10.1016/0968-0004(85)90270-1
State	Published - Mar 1985

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology

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10.1016/0968-0004(85)90270-1

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title = "Helix movements in proteins",

abstract = "Close-packed α-helices in proteins can move relative to each other by up to ∼1.5 {\AA} by small conformational adjustments in the side-chains that form the interface between them. Such relative helix motions facilitate the long-range transmission of conformational change, examples of which are the closure of clefts between domains in enzymes, and allosteric transitions.",

author = "Cyrus Chothia and Lesk, {Arthur M.}",

year = "1985",

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doi = "10.1016/0968-0004(85)90270-1",

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journal = "Trends in Biochemical Sciences",

issn = "0968-0004",

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AU - Chothia, Cyrus

AU - Lesk, Arthur M.

PY - 1985/3

Y1 - 1985/3

N2 - Close-packed α-helices in proteins can move relative to each other by up to ∼1.5 Å by small conformational adjustments in the side-chains that form the interface between them. Such relative helix motions facilitate the long-range transmission of conformational change, examples of which are the closure of clefts between domains in enzymes, and allosteric transitions.

AB - Close-packed α-helices in proteins can move relative to each other by up to ∼1.5 Å by small conformational adjustments in the side-chains that form the interface between them. Such relative helix motions facilitate the long-range transmission of conformational change, examples of which are the closure of clefts between domains in enzymes, and allosteric transitions.

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U2 - 10.1016/0968-0004(85)90270-1

DO - 10.1016/0968-0004(85)90270-1

M3 - Review article

AN - SCOPUS:0000195191

SN - 0968-0004

VL - 10

SP - 116

EP - 118

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

IS - 3

ER -

Helix movements in proteins

Abstract

All Science Journal Classification (ASJC) codes

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