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Grindley_NigelA unifying theme of Dr. Grindley's research is the study of enzymes that make and break phosphodiester bonds in DNA. His research focuses on the detailed biochemical mechanisms of (i) site-specific recombination mediated by the prototypical serine recombinase, γδ resolvase, and (ii) DNA synthesis and degradation mediated by the DNA polymerases Pol I (of E. coli), a highly accurate family A polymerase, and Dbh, an inaccurate family Y polymerase, which acts specifically to bypass damaged bases in the template strand during replication. In all three cases, he has detailed structural information obtained through collaborations with the X-ray crystallography group of Tom Steitz. In addition to using standard biochemical methods, he has recently added fluorescence techniques to dissect the biochemical pathways and define the nature and the role of the conformational transitions that take place during the processes of recombination or polymerase action.

 

Website: http://bbs.yale.edu/people/nigel_grindley-3.profile

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