2011
Efficient Discovery of Potent Anti-HIV Agents Targeting the Tyr181Cys Variant of HIV Reverse Transcriptase
Jorgensen WL, Bollini M, Thakur VV, Domaoal RA, Spasov KA, Anderson KS. Efficient Discovery of Potent Anti-HIV Agents Targeting the Tyr181Cys Variant of HIV Reverse Transcriptase. Journal Of The American Chemical Society 2011, 133: 15686-15696. PMID: 21853995, PMCID: PMC3183387, DOI: 10.1021/ja2058583.Peer-Reviewed Original ResearchConceptsHuman immunodeficiency virusWild-type HIV-1HIV-1Potent Anti-HIV AgentsInfected human T cellsNon-nucleoside reverseAnti-HIV AgentsHuman T cellsHIV reverse transcriptaseImmunodeficiency virusT cellsHIV RTViral strainsHIV agentsPresent reportReverse transcriptaseNM potencyCritical contributorPotential benefits
2007
From Docking False-Positive to Active Anti-HIV Agent
Barreiro G, Kim JT, Guimarães CR, Bailey CM, Domaoal RA, Wang L, Anderson KS, Jorgensen WL. From Docking False-Positive to Active Anti-HIV Agent. Journal Of Medicinal Chemistry 2007, 50: 5324-5329. PMID: 17918923, PMCID: PMC2575345, DOI: 10.1021/jm070683u.Peer-Reviewed Original ResearchWhy Urea Eliminates Ammonia Rather than Hydrolyzes in Aqueous Solution
Alexandrova AN, Jorgensen WL. Why Urea Eliminates Ammonia Rather than Hydrolyzes in Aqueous Solution. The Journal Of Physical Chemistry B 2007, 111: 720-730. PMID: 17249815, PMCID: PMC2995377, DOI: 10.1021/jp066478s.Peer-Reviewed Original ResearchConceptsAddition/elimination mechanismDecomposition of ureaWater moleculesResonance stabilizationAqueous solutionNH3 eliminationNatural bond order analysisQM/MM Monte Carlo simulationsBond order analysisFree energy perturbation calculationsQM/MMExplicit water modelRate-determining stepElimination mechanismOverall free energyLow activation energySolvent effectsElimination reactionHydrogen bondsPreferred reaction routeReaction routeGas phaseTransition stateZwitterionic intermediateAb initio
2004
Relationship between Side Chain Structure and 14-Helix Stability of β3-Peptides in Water
Kritzer JA, Tirado-Rives J, Hart SA, Lear JD, Jorgensen WL, Schepartz A. Relationship between Side Chain Structure and 14-Helix Stability of β3-Peptides in Water. Journal Of The American Chemical Society 2004, 127: 167-178. PMID: 15631466, PMCID: PMC2873033, DOI: 10.1021/ja0459375.Peer-Reviewed Original ResearchConceptsAlpha-helix foldingSide chain structureChain structureSolution-phase calculationsClass of foldamersSide-chain hydrogen bondingSide-chain carbonsAlpha-amino acidsHydrogen bondingΒ3‐PeptidesMacromolecular targetsChain carbonsRational designSuch moleculesConsiderable current interestDiverse functionalitiesFoldamersAlpha-helix propensityPolymersExperimental trendsAmino acidsSimilar versatilityAcidHomothreonineStructure