Models of natural mutations including site heterogeneity

New computational models of natural site mutations are developed that account for the different selective pressures acting on different locations in the protein. The number of adjustable parameters is greatly reduced by basing the models on the underlying physical‐chemical properties of the amino ac...

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Published inProteins, structure, function, and bioinformatics Vol. 32; no. 3; pp. 289 - 295
Main Authors Koshi, Jeffrey M., Goldstein, Richard A.
Format Journal Article
LanguageEnglish
Published Hoboken Wiley Subscription Services, Inc., A Wiley Company 15.08.1998
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Summary:New computational models of natural site mutations are developed that account for the different selective pressures acting on different locations in the protein. The number of adjustable parameters is greatly reduced by basing the models on the underlying physical‐chemical properties of the amino acids. This allows us to use our method on small data sets built of specific protein types. We demonstrate that with this approach we can represent the evolutionary patterns in HIV envelope proteins far better than with more traditional methods. Proteins 32:289–295, 1998. © 1998 Wiley‐Liss, Inc.
Bibliography:NSF - No. Equipment grant BIR9512955
istex:5FCAF6CD0F544FC8667A87A356283B7A975F1CAC
ArticleID:PROT4
College of Literature, Science, and the Arts, the Program in Protein Structure and Design, the Horace H. Rackham School of Graduate Studies
National Institutes of Health - No. GM08270; No. LM0577
ark:/67375/WNG-5BPN4KN6-X
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:0887-3585
1097-0134
DOI:10.1002/(SICI)1097-0134(19980815)32:3<289::AID-PROT4>3.0.CO;2-D