Representation of short and long-range handedness in protein structures by signed distance maps

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24 Scopus citations

Abstract

A new representation is proposed of short and long-range handedness in protein structures, by signed distance maps. This representation, based on the co-ordinates of the Cα atoms of proteins, does not require the assignment of specific regular structures. The short-range handedness along the chain in α-helical, β-strand and turn segments is shown, as well as the handedness between two strands of β-sheet structures and for crossover connections. Results are given for a βαβαβ folding unit of flavodoxin, a βαβ unit of subtilisin, which contains a left-handed crossover connection, and the domain 1 of bovine β-trypsin.

Original languageEnglish (US)
Pages (from-to)613-621
Number of pages9
JournalJournal of Molecular Biology
Volume163
Issue number4
DOIs
StatePublished - Feb 5 1983
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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