Fast protein fold recognition via sequence to structure alignment and contact capacity potentials

Pac Symp Biocomput. 1996:53-72.

Abstract

We propose new empirical scoring potentials and associated alignment procedures for optimally aligning protein sequences to protein structures. The method has two main applications: first, the recognition of a plausible fold for a protein sequence of unknown structure out of a database of representative protein structures and, second, the improvement of sequence alignments by using structural information in order to find a better starting point for homology based modelling. The empirical scoring function is derived from an analysis of a nonredundant database of known structures by converting relative frequencies into pseudoenergies using a normalization according to the inverse Bolzmann law. These-so called contact capacity-potentials turn out to be discriminative enough to detect structural folds in the absence of significant sequence similarity and at the same time simple enough to allow for a very fast optimization in an alignment procedure.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Algorithms
  • Amino Acid Sequence
  • Computer Simulation
  • Databases, Factual
  • Molecular Sequence Data
  • Protein Folding*
  • Protein Structure, Secondary*
  • Proteins / chemistry*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Software
  • Thermodynamics

Substances

  • Proteins