1993
The structural enzymology of proton-transfer reactions
Petsko G, Ringe D, Allen K, Lavie A, Gerhart-Mueller E, Clifton J, Hasson M, Fujita S, Sugio S, Xhang X, Davenport R, Lolis E, Neidhart D, Kenyon G, Gerlt J, Knowles J, Bash P, Karplus M. The structural enzymology of proton-transfer reactions. Protein Engineering Design And Selection 1993, 6: 37-37. DOI: 10.1093/protein/6.supplement.37-a.Peer-Reviewed Original ResearchProton-transfer reactionsProton transfer reactionsEfficient proton transferX-ray crystallographyMolecular dynamics simulationsProton transferTransfer reactionsChemical transformationsLow pKaDynamics simulationsEnzymic baseX-rayOptimal catalysisStructural featuresCarbonic acidReactionStructural enzymologyPKaCrystallographyCatalysisSite-directed mutagenesisHydrogenProtonChemicalCarbon
1990
Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.
Lolis E, Petsko G. Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis. Biochemistry 1990, 29: 6619-25. PMID: 2204418, DOI: 10.1021/bi00480a010.Peer-Reviewed Original ResearchConceptsHydrogen bondsSide chainsGlu-165Triosephosphate isomeraseLatter hydrogen bondTransition state analogueFinal R factorEnzyme-inhibitor complexSpectroscopic resultsActive siteConformational changesCrystallographic analysisLoop movesPhosphoglycolic acidIsomeraseUnbound formCatalysisR factorBondsEnzymeComplexesStructural termsAtomic modelBindingChainTransition-State Analogues in Protein Crystallography: Probes of the Structural Source of Enzyme Catalysis
Lolis E, Petsko G. Transition-State Analogues in Protein Crystallography: Probes of the Structural Source of Enzyme Catalysis. Annual Review Of Biochemistry 1990, 59: 597-630. PMID: 2197984, DOI: 10.1146/annurev.bi.59.070190.003121.Peer-Reviewed Original Research