Unit

UNIT 2.2 Hydrophobicity Profiles for Protein Sequence Analysis

  1. Stanley R. Krystek Jr.,
  2. William J. Metzler,
  3. Jiri Novotny

Published Online: 1 MAY 2001

DOI: 10.1002/0471140864.ps0202s00

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Krystek, S. R., Metzler, W. J. and Novotny, J. 2001. Hydrophobicity Profiles for Protein Sequence Analysis. Current Protocols in Protein Science. 00:2.2:2.2.1–2.2.13.

Author Information

  1. Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey

Publication History

  1. Published Online: 1 MAY 2001
  2. Published Print: JUN 1995

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.