1998
Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus‐8 MIP‐II
Shao W, Fernandez E, Wilken J, Thompson D, Siani M, West J, Lolis E, Schweitzer B. Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus‐8 MIP‐II. FEBS Letters 1998, 441: 77-82. PMID: 9877169, DOI: 10.1016/s0014-5793(98)01520-8.Peer-Reviewed Original ResearchConceptsTotal chemical synthesisNuclear magnetic resonanceChemical synthesisX-ray crystallographyThree-dimensional structureStructural studiesSynthesisSecondary structureGenome programNew proteinsMagnetic resonanceSelenomethionine proteinsRecombinant proteinsProtein IIHeavy-atom derivativesProteinMIP IICrystallographyMonomersStructureDeterminationDerivativesCloningHigh resolutionResonance
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
Transition-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