Helix movements in proteins

Cyrus Chothia, Arthur Lesk

Research output: Contribution to journalReview article

64 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 languageEnglish (US)
Pages (from-to)116-118
Number of pages3
JournalTrends in Biochemical Sciences
Volume10
Issue number3
DOIs
StatePublished - Jan 1 1985

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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