A priori and a posteriori mixture distributions for using databases in protein structure determination

Stanley L. Sclove, Simon Sherman

Research output: Contribution to journalArticle

2 Scopus citations


The twists and turns of protein molecules correspond to the rotational angles of the main and side chains in their constituent amino acid residues. Owing to stereochemical restrictions the joint distribution of these angles falls into several well-separated clusters. Consequently, we fit a statistical finite mixture model to data from the Brookhaven Protein Data Bank (PDB), obtaining a new classification of conformational states of amino acids. The results of this database modeling are important for knowledge-based approaches to protein structure determination and analysis and can be used in conjunction with experimental data in the determination of protein spatial structure. As part of this process, the mixture distributions we have fit can be used as a priori distributions. A posteriori distributions corresponding to these a priori mixture distributions are illustrated.

Original languageEnglish (US)
Pages (from-to)245-255
Number of pages11
JournalJournal of Molecular Structure: THEOCHEM
Issue number1-3
Publication statusPublished - Dec 8 1997



  • A priori and a posteriori distributions
  • Cluster analysis
  • Protein local structure determination
  • Statistical finite mixture model

ASJC Scopus subject areas

  • Biochemistry
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

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