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S.J. Remington

Researcher at University of Oregon

Publications -  46
Citations -  6044

S.J. Remington is an academic researcher from University of Oregon. The author has contributed to research in topics: Citrate synthase & Protein structure. The author has an hindex of 32, co-authored 46 publications receiving 5832 citations. Previous affiliations of S.J. Remington include Max Planck Society.

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Proposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A.

TL;DR: A mechanism for the condensation reaction is proposed which involves the participation of three key catalytic groups in two distinct steps and invokes concerted general acid-base catalysis twice to explain both the energetics of the reaction and the experimentally observed inversion of stereochemistry at the attacking carbon atom.
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Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design.

TL;DR: The structures of AmpC beta-lactamase from Escherichia coli, alone and in complex with a transition-state analogue, and the structure of the m-aminophenylboronic acid adduct suggest several ways to improve the affinity of this class of inhibitor and points to the existence of several unusual binding-site-like features in the region of the AmpC catalytic site.
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The structure of rat mast cell protease II at 1.9-A resolution.

TL;DR: The structure of rat mast cell protease II, a serine protease with chymotrypsin-like primary specificity, has been determined and forms a basis for an explanation of the unusual properties of other members of this class.
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Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetonyl-coenzyme A.

TL;DR: The crystal structure of the complex of pig heart citrate synthase and oxaloacetate in the presence of the potent inhibitor S-acetonyl coenzyme A has been determined at a nominal resolution of 2.9 A by Patterson search techniques and refined by restrained crystallographic refinement to conclude that this is a third structural state of the enzyme.
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Relation between hen egg white lysozyme and bacteriophage T4 lysozyme: evolutionary implications.

TL;DR: Structural and functional similarities suggest that the two lysozymes have arisen by divergent evolution from a common precursor, the first case in which two proteins of completely different amino acid sequence have been shown, with high probability, to have evolved by Divergent rather than convergent evolution.