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Amino acid substitution matrices from protein blocks. Howard Hughes Medical Institute, Fred Hutchinson Cancer Research Center, Seattle, WA 98104. This article has been cited by other articles in PMC.Abstract Methods for alignment of protein sequences typically measure similarity by using a substitution matrix with scores for all possible exchanges of one amino acid with another. The most widely used matrices are based on the Dayhoff model of evolutionary rates. Using a different approach, we have derived substitution matrices from about 2000 blocks of aligned sequence segments characterizing more than 500 groups of related proteins. This led to marked improvements in alignments and in searches using queries from each of the groups. Full text Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.0M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References. Selected References These references are in PubMed. This may not be the complete list of references from this article.
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