期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 27, 期 6, 页码 315-321出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/S0968-0004(02)02094-7
关键词
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资金
- NIGMS NIH HHS [R01 GM 62118] Funding Source: Medline
Most modern tools that analyze protein evolution allow individual sites to mutate at constant rates over the history of the protein family. However, Walter Fitch observed in the 1970s that, if a protein changes its function, the mutability of individual sites might also change. This observation is captured in the 'non-homogeneous gamma model', which extracts functional information from gene families by examining the different rates at which individual sites evolve. This model has recently been coupled with structural and molecular biology to identify sites that are likely to be involved in changing function within the gene family. Applying this to multiple gene families highlights the widespread divergence of functional behavior among proteins to generate paralogs and orthologs.
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