2021
Enhanced specificity mutations perturb allosteric signaling in CRISPR-Cas9
Nierzwicki L, East K, Morzan U, Arantes P, Batista V, Lisi G, Palermo G. Enhanced specificity mutations perturb allosteric signaling in CRISPR-Cas9. ELife 2021, 10: e73601. PMID: 34908530, PMCID: PMC8741213, DOI: 10.7554/elife.73601.Peer-Reviewed Original ResearchConceptsHNH domainAllosteric communicationCatalytic HNH domainDNA recognition regionSpecificity-enhancing mutationsGenome editing capabilitiesAllosteric signalingAllosteric signalMutations perturbAllosteric hotspotsSpecificity enhancementCas9 endonucleaseMutational studiesDNA recognitionAllosteric connectivityAllosteric roleMolecular toolsAllosteric structureRecognition regionMolecular levelBiochemical studiesDNA cleavageSolution NMRMutationsCatalytic siteComputational insights into the membrane fusion mechanism of SARS-CoV-2 at the cellular level
Wang J, Maschietto F, Guberman-Pfeffer MJ, Reiss K, Allen B, Xiong Y, Lolis E, Batista VS. Computational insights into the membrane fusion mechanism of SARS-CoV-2 at the cellular level. Computational And Structural Biotechnology Journal 2021, 19: 5019-5028. PMID: 34540146, PMCID: PMC8442599, DOI: 10.1016/j.csbj.2021.08.053.Peer-Reviewed Original ResearchMembrane fusion mechanismMembrane fusionSpike trimerNeutral amino acid transporterHost cellular membranesAmino acid transportersCentral stalkCentral poreHost membraneFusion mechanismCellular membranesAcid transportersMolecular levelViral membraneCellular levelEnzymatic activityChoreographic eventFusion peptideAntiviral inhibitorsDrug designAttractive targetInitial bindingMembraneConformational constraintsSpike glycoprotein
2017
Charge Transport and Rectification in Donor–Acceptor Dyads
Hedström S, Matula A, Batista V. Charge Transport and Rectification in Donor–Acceptor Dyads. The Journal Of Physical Chemistry C 2017, 121: 19053-19062. DOI: 10.1021/acs.jpcc.7b05749.Peer-Reviewed Original ResearchFrontier orbitalsConjugated donor–acceptor systemA systemDensity functional theory levelDonor-acceptor dyadsDonor-acceptor systemsAppropriate transport propertiesGold electrodeA dyadsMolecular conformationTransport propertiesMolecular junctionsTheory levelRational designPhotovoltaic devicesCharge transportStructure-function relationshipsChemical compositionLarge rectification ratioOrbitalsFundamental physical insightsMolecular levelRectification propertiesRectification ratioFermi level
2013
Spectral Tuning of Ultraviolet Cone Pigments: An Interhelical Lock Mechanism
Sekharan S, Mooney V, Rivalta I, Kazmi M, Neitz M, Neitz J, Sakmar T, Yan E, Batista V. Spectral Tuning of Ultraviolet Cone Pigments: An Interhelical Lock Mechanism. Journal Of The American Chemical Society 2013, 135: 19064-19067. PMID: 24295328, PMCID: PMC4536979, DOI: 10.1021/ja409896y.Peer-Reviewed Original ResearchConceptsUV pigmentsCone pigmentsSpectral tuningActivation of rhodopsinAncestral pigmentMolecular evolutionVertebrate visionMutagenesis studiesPhotoreceptor rhodopsinMolecular levelStructural rearrangementsUnprotonated Schiff baseTransmembraneTM6PigmentsRhodopsinMutationsEssential componentRetinyl chromophoreHydrogen bonding networkMutantsTM2Structural modelPhysiologicalRearrangementSpectral Tuning in Halorhodopsin: The Chloride Pump Photoreceptor
Pal R, Sekharan S, Batista V. Spectral Tuning in Halorhodopsin: The Chloride Pump Photoreceptor. Journal Of The American Chemical Society 2013, 135: 9624-9627. PMID: 23777372, DOI: 10.1021/ja404600z.Peer-Reviewed Original ResearchConceptsKey amino acid residuesIon translocation pathwayAmino acid residuesSpectral tuningInternal water moleculesTranslocation pathwaySpecific hydrogen bondsHalobacterium salinarumAcid residuesMolecular levelStructural rearrangementsAnion transportCl depletionPhotoreceptorsInduces changesHalorhodopsinRetinyl chromophoreSalinarumMutationsResiduesPathwayFirst time