title: Identification of protein folds: matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structures.
abstract: Hydrophobic side chains often are buried in the interior of a protein, and evolutionarily related proteins usually maintain the hydrophobic character of buried positions. In this paper we show 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 data base of protein structures.
authors.affiliation: Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
authors.forename: J U
authors.initials: JU
authors.lastname: Bowie
authors.forename: N D
authors.initials: ND
authors.lastname: Clarke
authors.forename: C O
authors.initials: CO
authors.lastname: Pabo
authors.forename: R T
authors.initials: RT
authors.lastname: Sauer
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D003574:Cytochrome c Group; D007256:Information Systems; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012995:Solubility
chemical_list: D001426:Bacterial Proteins; D003574:Cytochrome c Group; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins