Title |
The non-random clustering of non-synonymous substitutions and its relationship to evolutionary rate
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Published in |
BMC Genomics, August 2011
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DOI | 10.1186/1471-2164-12-415 |
Pubmed ID | |
Authors |
Lisa G McFerrin, Eric A Stone |
Abstract |
Protein sequences are subject to a mosaic of constraint. Changes to functional domains and buried residues, for example, are more apt to disrupt protein structure and function than are changes to residues participating in loops or exposed to solvent. Regions of constraint on the tertiary structure of a protein often result in loose segmentation of its primary structure into stretches of slowly- and rapidly-evolving amino acids. This clustering can be exploited, and existing methods have done so by relying on local sequence conservation as a signature of selection to help identify functionally important regions within proteins. We invert this paradigm by leveraging the regional nature of protein structure and function to both illuminate and make use of genome-wide patterns of local sequence conservation. |
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Demographic breakdown
Readers by professional status | Count | As % |
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Professor > Associate Professor | 4 | 10% |
Student > Bachelor | 3 | 8% |
Student > Master | 3 | 8% |
Other | 6 | 15% |
Unknown | 3 | 8% |
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Medicine and Dentistry | 1 | 3% |
Other | 0 | 0% |
Unknown | 5 | 13% |