Predicting protein conformation by statistical methods

István Simon, András Fiser, Gábor E. Tusnády

Research output: Contribution to journalReview article

15 Scopus citations

Abstract

The unique folded structure makes a polypeptide a functional protein. The number of known sequences is about a hundred times larger than the number of known structures and the gap is increasing rapidly. The primary goal of all structure prediction methods is to obtain structure-related information on proteins, whose structures have not been determined experimentally. Besides this goal, the development of accurate prediction methods helps to reveal principles of protein folding. Here we present a brief survey of protein structure predictions based on statistical analyses of known sequence and structure data. We discuss the background of these methods and attempt to elucidate principles, which govern structure formation of soluble and membrane proteins.

Original languageEnglish (US)
Pages (from-to)123-136
Number of pages14
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1549
Issue number2
DOIs
Publication statusPublished - Oct 18 2001

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Keywords

  • Amino acid sequence
  • Prediction
  • Protein
  • Statistical method
  • Structure
  • Topology
  • Transmembrane protein

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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