Identification of protein folds: matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structures.
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.
Bowie
J U
JU
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Clarke
N D
ND
Pabo
C O
CO
Sauer
R T
RT
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
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins