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Robert C. Davenport
Researcher at Brandeis University
Publications - 8
Citations - 951
Robert C. Davenport is an academic researcher from Brandeis University. The author has contributed to research in topics: Triosephosphate isomerase & Site-directed mutagenesis. The author has an hindex of 7, co-authored 8 publications receiving 937 citations. Previous affiliations of Robert C. Davenport include Massachusetts Institute of Technology.
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Journal ArticleDOI
Structure of yeast triosephosphate isomerase at 1.9-A resolution.
TL;DR: Analysis of the subunit interface of this dimeric enzyme hints at the source of the specificity of one subunit for another and allows us to estimate an association constant of 10(14)-10(16) M-1 for the two monomers, which suggests that the interface may be a particularly good target for drug design.
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Computer simulation and analysis of the reaction pathway of triosephosphate isomerase
Paul A. Bash,Martin J. Field,Robert C. Davenport,Gregory A. Petsko,Dagmar Ringe,Martin Karplus +5 more
TL;DR: The results suggest that, although Lys-12 is most important, many other residues within 16 A of the substrate contribute and that histidine-95 as the imidazole/imidazolate pair could act as an acid/base catalyst.
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Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway.
Robert C. Davenport,Paul A. Bash,Barbara A. Seaton,Martin Karplus,Gregory A. Petsko,Dagmar Ringe +5 more
TL;DR: The three-dimensional structure of TIM complexed with a reactive intermediate analogue, phosphoglycolohydroxamate (PGH), is solved at 1.9-A resolution and the structure suggests that His-95 is neutral rather than cationic in the ground state and therefore would have to function as an imidazole acid instead of the usualImidazolium.
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Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism.
TL;DR: Tritium exchange experiments similar to those used to define the free energy profile for the wild-type yeast isomerase, together with a new method of analysis involving 14C and 3H doubly labeled substrates, have been used to investigate the energetics of the mutants catalyzed reaction.
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Subunit interface of triosephosphate isomerase: site-directed mutagenesis and characterization of the altered enzyme
TL;DR: This mutant enzyme was less resistant than wild-type TIM to denaturation and inactivation caused by elevated temperature, denaturants, tetrabutylammonium bromide, alkaline pH, and proteases.