Determinants of protein function revealed by combinatorial entropy optimization Journal Article


Authors: Reva, B.; Antipin, Y.; Sander, C.
Article Title: Determinants of protein function revealed by combinatorial entropy optimization
Abstract: We use a new algorithm (combinatorial entropy optimization [CEO]) to identify specificity residues and functional subfamilies in sets of proteins related by evolution. Specificity residues are conserved within a subfamily but differ between subfamilies, and they typically encode functional diversity. We obtain good agreement between predicted specificity residues and experimentally known functional residues in protein interfaces. Such predicted functional determinants are useful for interpreting the functional consequences of mutations in natural evolution and disease. © 2007 Reva et al.; licensee BioMed Central Ltd.
Keywords: gene mutation; genetics; nonhuman; molecular genetics; protein domain; protein function; protein analysis; cell cycle protein; cell cycle proteins; algorithms; physiology; evolution, molecular; chemistry; molecular evolution; amino acid sequence; molecular sequence data; sequence homology, amino acid; algorithm; sequence alignment; binding site; ras protein; protein structure; sequence homology; protein family; phosphotransferase; genetic conservation; combinatorial chemistry; combinatorial chemistry techniques; gtp phosphohydrolases; guanosine triphosphatase; combinatorial entropy optimization; entropy
Journal Title: Genome Biology
Volume: 8
Issue: 11
ISSN: 1465-6906
Publisher: Biomed Central Ltd  
Date Published: 2007-11-01
Start Page: R232
Language: English
DOI: 10.1186/gb-2007-8-11-r232
PUBMED: 17976239
PROVIDER: scopus
PMCID: PMC2258190
DOI/URL:
Notes: --- - "Cited By (since 1996): 37" - "Export Date: 17 November 2011" - "CODEN: GNBLF" - "Source: Scopus"
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  1. Boris A Reva
    36 Reva
  2. Chris Sander
    210 Sander
  3. Yevgeniy Antipin
    19 Antipin