Predicting the helix packing of globular proteins by self‐correcting distance geometry

C. H. Mumenthaler, W. Braun

Research output: Contribution to journalArticle

48 Scopus citations

Abstract

A new self‐correcting distance geometry method for predicting the three‐dimensional structure of small globular proteins was assessed with a test set of 8 helical proteins. With the knowledge of the amino acid sequence and the helical segments, our completely automated method calculated the correct backbone topology of six proteins. The accuracy of the predicted structures ranged from 2.3 Å to 3.1 Å for the helical segments compared to the experimentally determined structures. For two proteins, the predicted constraints were not restrictive enough to yield a conclusive prediction. The method can be applied to all small globular proteins, provided the secondary structure is known from NMR analysis or can be predicted with high reliability.

Original languageEnglish (US)
Pages (from-to)863-871
Number of pages9
JournalProtein Science
Volume4
Issue number5
DOIs
StatePublished - May 1995
Externally publishedYes

Keywords

  • DIAMOD
  • distance geometry in torsion angles
  • helix bundles
  • multiple sequence alignment
  • tertiary structure prediction
  • variable target function method

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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