Protein conformational in higher order φ-ψ maps

Gregory E. Sims, In-Geol Choi, Sung Hou Kim

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

We have mapped protein conformational space from two to seven residue lengths by employing multidimensional scaling on a data matrix composed of pair-wise angular distances for multiple φ-ψ values collected from high-resolution protein structures. The resulting global maps show clustering of peptide conformations that reveals a dramatic reduction of conformational space as sampled by experimentally observed peptides. Each map can be viewed as a higher order φ-ψ plot defining regions of space that are conformationally allowed.

Original languageEnglish
Pages (from-to)618-621
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume102
Issue number3
DOIs
Publication statusPublished - 2005 Jan 18
Externally publishedYes

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Peptides
Cluster Analysis
Proteins

Keywords

  • Global mapping
  • Global peptide conformational mapping
  • Multidimensional scaling
  • Ramachandran map

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Protein conformational in higher order φ-ψ maps. / Sims, Gregory E.; Choi, In-Geol; Kim, Sung Hou.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 102, No. 3, 18.01.2005, p. 618-621.

Research output: Contribution to journalArticle

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