title: Hydrophobicity profiles for protein sequence analysis.
abstract: Hydrophobic interactions are a major force in protein folding and numerous hydropathy scales have been developed to quantify the relative hydrophobicity of the amino acids. Hydropathy profiles can be used to examine the surface features of proteins in order to generate hypotheses that can be confirmed experimentally. This unit describes the application of hydrophobicity plots to typical problems and provides suggested uses for a few selected scales.
authors.affiliation: Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey, USA.
authors.forename: S R
authors.initials: SR
authors.lastname: Krystek
authors.forename: W J
authors.initials: WJ
authors.lastname: Metzler
authors.forename: J
authors.initials: J
authors.lastname: Novotny
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D020539:Sequence Analysis, Protein / Q000379:methods*
chemical_list: D011506:Proteins