title: Prediction of polypeptide fragments exposed to the solvent.
abstract: A method is presented to predict those polypeptide segments within a globular protein that are more likely to be exposed to the solvent. The protein amino acidic sequence is the only information needed by this new algorithm. It uses a consensus hydrophobicity scale, derived from 28 known scales, and it is based on the comparison between the average hydrophobicity of a polypeptide fragment and the average hydrophobicity expected for a segment containing the same number of residues. The latter values are pre-computed from a non-redundant set of single chain protein structural domains. The comparison between the two average values results in a t value that readily provides the prediction with a statistical significance. A jack-knife validation analysis indicates that the protein segment predicted to be the most solvent exposed is actually solvent exposed and amongst the fragments that are most exposed. The source of a stand-alone program, written in C language, that allows the prediction of the most likely solvent exposed segment in a globular protein is available from the author.
authors.affiliation: Department of General Chemistry of the Pavia University, Viale Taramelli 12, I-27100 Pavia, Italy. carugo@embl-heidelberg.de
authors.forename: Oliviero
authors.initials: O
authors.lastname: Carugo
mesh_terms: D000465:Algorithms; D000596:Amino Acids / Q000737:chemistry; D003198:Computer Simulation; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D012984:Software; D012997:Solvents
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D011506:Proteins; D012997:Solvents