2021
Cellular Sticking Can Strongly Reduce Complex Binding by Speeding Dissociation
Davis C, Gruebele M. Cellular Sticking Can Strongly Reduce Complex Binding by Speeding Dissociation. The Journal Of Physical Chemistry B 2021, 125: 3815-3823. PMID: 33826329, DOI: 10.1021/acs.jpcb.1c00950.Peer-Reviewed Original ResearchConceptsSpliceosomal protein U1APotential binding partnerMajor cellular effectsProtein U1ABinding partnerU1 snRNACellular environmentNonspecific interactionsFörster resonance energy transferProper bindingCellular componentsResonance energy transferU1ALive cellsLarge hydrophobic surface areaMacromolecular crowdingCellular effectsHydrophobic surface areaOS cellsModel systemComplex bindingHigh binding affinityWeak nonspecific interactionsBinding affinitiesCells
2019
A programmable DNA-origami platform for studying lipid transfer between bilayers
Bian X, Zhang Z, Xiong Q, De Camilli P, Lin C. A programmable DNA-origami platform for studying lipid transfer between bilayers. Nature Chemical Biology 2019, 15: 830-837. PMID: 31320758, PMCID: PMC6650167, DOI: 10.1038/s41589-019-0325-3.Peer-Reviewed Original ResearchConceptsLipid transferNon-vesicular lipid transportSynaptotagmin-like mitochondrial lipid-binding protein (SMP) domainLipid transportMembrane contact sitesLipid transport proteinsSMP domainImportant physiological roleDNA origami platformProtein domainsUnstructured linkerContact sitesSynaptotagmin-1Förster resonance energy transferPhysiological roleResonance energy transferMechanistic insightsDNA origami nanostructuresAcceptor liposomes
2016
Snapshot of sequential SNARE assembling states between membranes shows that N-terminal transient assembly initializes fusion
Wang YJ, Li F, Rodriguez N, Lafosse X, Gourier C, Perez E, Pincet F. Snapshot of sequential SNARE assembling states between membranes shows that N-terminal transient assembly initializes fusion. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: 3533-3538. PMID: 26979957, PMCID: PMC4822643, DOI: 10.1073/pnas.1518935113.Peer-Reviewed Original ResearchConceptsFörster resonance energy transferProminent biological processesIntermembrane spaceSNARE proteinsTransmembrane complexTerminal domainInvolved proteinsBiological processesTransient assemblyResonance energy transferProteinSnareIntermembrane distanceMembraneAssemblyMolecular assembliesPathwayComplexes
2013
Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics
Xia S, Wood M, Bradley MJ, De La Cruz EM, Konigsberg WH. Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics. Nucleic Acids Research 2013, 41: 9077-9089. PMID: 23921641, PMCID: PMC3799440, DOI: 10.1093/nar/gkt674.Peer-Reviewed Original ResearchConceptsRB69 DNA polymeraseFörster resonance energy transferDNA polymeraseHigh-resolution X-ray crystallographyResolution X-ray crystallographyHigh mutation rateB-family polConformational dynamicsExonuclease domainState kinetic parametersMutation rateG mutantResonance energy transferX-ray crystallographyM variantPolymerasePrimer terminusHydrophobic cavityActive siteBase selectivitySimilar substitutionSide chainsProfound effectDramatic effectInternal cavity
2010
Combinatorial Cysteine Mutagenesis Reveals a Critical Intramonomer Role for Cysteines in Prestin Voltage Sensing
Bai JP, Surguchev A, Bian S, Song L, Santos-Sacchi J, Navaratnam D. Combinatorial Cysteine Mutagenesis Reveals a Critical Intramonomer Role for Cysteines in Prestin Voltage Sensing. Biophysical Journal 2010, 99: 85-94. PMID: 20655836, PMCID: PMC2895379, DOI: 10.1016/j.bpj.2010.03.066.Peer-Reviewed Original ResearchConceptsDisulfide bond formationCysteine residuesCysteine residue pairsSingle cysteine residueCysteine mutagenesisTransmembrane proteinSubstitution mutantsSLC26 familyResidue pairsFörster resonance energy transferCharge movementVoltage-dependent charge movementDisulfide interactionsResonance energy transferPrestinProteinMutantsDimer formationResiduesCysteineHair cellsSurface expressionAnion transportersCochlear amplificationWestern blot
1999
Detergents modulate dimerization, but not helicity, of the glycophorin A transmembrane domain 11Edited by G. von Heijne
Fisher L, Engelman D, Sturgis J. Detergents modulate dimerization, but not helicity, of the glycophorin A transmembrane domain 11Edited by G. von Heijne. Journal Of Molecular Biology 1999, 293: 639-651. PMID: 10543956, DOI: 10.1006/jmbi.1999.3126.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceButyratesCircular DichroismDetergentsDimerizationEnergy TransferFluorescent DyesGlycophorinsHumansKineticsMicellesMolecular Sequence DataPeptide FragmentsPhosphorylcholineProtein Structure, SecondaryQuaternary Ammonium CompoundsSodium Dodecyl SulfateSolventsSpectrometry, FluorescenceThermodynamicsConceptsSpecific chemical interactionsFörster resonance energy transferResonance energy transferSodium dodecyl sulfateComplex solventChemical interactionFar-UV circular dichroismCircular dichroismDodecyl sulfateTransmembrane helix associationDetergent micellesHelix associationEnergy transferThermodynamic measurementsHelix formationObserved KdZwitterionic detergentSecondary structureDimerizationG. von HeijneHelix dimerizationOrders of magnitudeDetergentsTransmembrane helicesTransmembrane domain
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