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Quantitative comparison of the ability of hydropathy scales to recognize surface β‐strands in proteins
Author(s) -
Palliser Christopher C.,
Parry David A. D.
Publication year - 2000
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/1097-0134(20010201)42:2<243::aid-prot120>3.0.co;2-b
Subject(s) - sequence (biology) , biological system , parry , computational biology , computer science , chemistry , biology , artificial intelligence , biochemistry
Methods based on the use of hydropathy scales have been used widely to ascertain the secondary structures of proteins. However, over 100 such scales have been reported in the literature, and which of these is the most successful in terms of the prediction rate of the correct structure is not clear. This article, therefore, reports a comprehensive analysis of the relative success of hydropathy scales to locate β‐strands on the surfaces of proteins. The technique we used is based on the technique proposed by Fraser and Parry, but it includes a modification that allows a higher rate of successful prediction and a lower rate of overprediction. We used as a basis for assessing the predictions a database of sequence‐unique structures that we previously established. Proteins 2001;42:243–255. © 2000 Wiley‐Liss, Inc.