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
1990
Structure of yeast triosephosphate isomerase at 1.9-A resolution.
Lolis E, Alber T, Davenport R, Rose D, Hartman F, Petsko G. Structure of yeast triosephosphate isomerase at 1.9-A resolution. Biochemistry 1990, 29: 6609-18. PMID: 2204417, DOI: 10.1021/bi00480a009.Peer-Reviewed Original ResearchConceptsHydrogen bonding interactionsYeast triosephosphate isomeraseActive site structureNon-hydrogen atomsWater moleculesActive siteActive site residuesDrug designGlu-165Triosephosphate isomeraseSite structureCatalytic baseCrystal contactsSite residuesR factorTIM structuresFlexible loopLys-12Polypeptide chainStructureSubunit interfaceCarboxylateMonomersHydroxylFirst time