Monday, July 11, 2011, 11:00 am — John Dunn Seminar Room, Bldg. 463
Protein folds are thought to evolve by gradual accumulation of small sequence mutations, giving rise to distantly related members with little conservation of either sequence or structure. Correlating sequence mutations with fold changes for such distant relatives is a major challenge, as background mutations obscure sequence differences important for specifying structure. In order to circumvent this problem, our lab combines sensitive sequence analysis with structural characterization to identify related proteins with significant sequence similarity yet different folds. In the example of the cro family of bacteriophage transcription factors, we have characterized two members with 40% sequence identity yet dramatically different secondary structure compositions. In a second example, two insect salivary lipocalins with direct sequence similarity exhibit fold differences interchangeable by beta strand flipping, slipping, and swapping. In both cases, combined sequence and structural analysis provides new insights into protein structure evolution.
Hosted by: Alexei Soares
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