Identification of protein folds: Matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structures

✍ Scribed by James U. Bowie; Neil D. Clarke; Carl O. Pabo; Robert T. Sauer

• Publisher: John Wiley and Sons
• Year: 1990
• Tongue: English
• Weight: 820 KB
• Volume: 7
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/prot.340070307

✦ Synopsis

Abstract

Hydrophobic side chains often are buried in the interior of a protein, and evolutionarily related proteins usually maintain the hydrophobic character of buried position. In this paper we shown that a pattern of hydrophobicity values derived from a set of related protein sequences is well correlated with the linear pattern of side‐chain solvent accessibility values, calculated from a known protein structure representative of the sequences. In several cases, information from aligned sequences can be used to select the correct tertiary fold from a large database of protein structures.