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 in | Proteins, structure, function, and bioinformatics Vol. 32; no. 3; pp. 289 - 295 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Hoboken
Wiley Subscription Services, Inc., A Wiley Company
15.08.1998
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Subjects | |
Online Access | Get full text |
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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. |
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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 |