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A simple method for displaying the hydropathic character of a protein-英文文献
J. Mol. Biol. (1982) 157, 105-132
A Simple Method for Displaying the Hydropathic
Character of a Protein
JACK KYTE AND RUSSELLF. DOOLITTLE
Department of Chemistry
University of California, San Diego, La Jolla, Calif. 92093, 1J.S.,4.
(Received 8 August 1981~ and in revised form 25 January 1982)
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
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