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A simple method for displaying the hydropathic character of a protein (1982)
| Venue: | Journal of Molecular Biology |
| Citations: | 2285 - 2 self |
BibTeX
@ARTICLE{Kyte82asimple,
author = {Jack Kyte and Russell and F. Doolittle},
title = {A simple method for displaying the hydropathic character of a protein},
journal = {Journal of Molecular Biology},
year = {1982}
}
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Abstract
A computer program that progressively evaluates the hydrophilicity and hydrophobicity of a protein along its amino acid sequence has been devised. For this purpose, a hydropathy scale has been composed wherein the hydrophilic and hydrophobic properties of each of the 20 amino acid side-chains is taken into consideration. The scale is based on an amalgam of experimental observations derived from the literature. The program uses a moving-segment approach that continuously determines the average hydropathy within a segment of predetermined length as it advances through the sequence. The consecutive scores are plotted from the amino to the carboxy terminus. At the same time, a midpoint line is printed that corresponds to the grand average of the hydropathy of the amino acid compositions found in most of the sequenced proteins. In the case of soluble, globular proteins there is a remarkable correspondence between the interior portions of their sequence and the regions appearing on the hydrophobic side of the midpoint line, as well as the exterior portions and the regions on the hydrophilic side. The correlation was demonstrated by comparisons between the plotted values and known structures determined by crystallography. In the case of membrane-bound proteins, the portions of their sequences that are located within the lipid bilayer are also clearly delineated by large uninterrupted areas on the hydrophobic side of the midpoint line. As such, the membrane-spanning segment’s of these proteins can be identified by this procedure. Although the method is not unique and embodies principles that have long been appreciated, its simplicity and its graphic nature make it a very useful tool for the evaluation of protein structures. 1.
Keyphrases
hydropathic character midpoint line simple method hydrophobic side sequenced protein useful tool embodies principle interior portion grand average consecutive score remarkable correspondence graphic nature exterior portion computer program experimental observation predetermined length hydropathy scale protein structure carboxy terminus amino acid sequence average hydropathy plotted value globular protein amino acid side-chains hydrophobic property moving-segment approach membrane-spanning segment amino acid composition hydrophilic side lipid bilayer large uninterrupted area membrane-bound protein
