2003
Amphipols: polymeric surfactants for membrane biology research
Popot J, Berry E, Charvolin D, Creuzenet C, Ebel C, Engelman D, Flötenmeyer M, Giusti F, Gohon Y, Hervé P, Hong Q, Lakey J, Leonard K, Shuman H, Timmins P, Warschawski D, Zito F, Zoonens M, Pucci B, Tribet C. Amphipols: polymeric surfactants for membrane biology research. Cellular And Molecular Life Sciences 2003, 60: 1559-1574. PMID: 14513831, PMCID: PMC11138540, DOI: 10.1007/s00018-003-3169-6.Peer-Reviewed Original ResearchConceptsMembrane proteinsQuasi-irreversible mannerPolymeric surfactantsAmphiphilic polymersMembrane biologyAqueous solutionTransmembrane surfaceAmphipolsBiology researchDissociating characterPutative usesNative stateSurfactantsNovel familyProteinCurrent knowledgeRapid inactivationNoncovalentDetergentsPolymersBiologyCompoundsComplexesInactivationAbsence
1996
Leucine side-chain rotamers in a glycophorin A transmembrane peptide as revealed by three-bond carbon—carbon couplings and 13C chemical shifts
MacKenzie K, Prestegard J, Engelman D. Leucine side-chain rotamers in a glycophorin A transmembrane peptide as revealed by three-bond carbon—carbon couplings and 13C chemical shifts. Journal Of Biomolecular NMR 1996, 7: 256-260. PMID: 8785502, DOI: 10.1007/bf00202043.Peer-Reviewed Original ResearchConceptsChemical shiftsPeptide dimersΑ-carbonSide chainsSide-chain rotamer populationsCarbon-carbon couplingLeucine side chainsThree-bond J couplingsNMR pulse sequencesΔ-methyl groupsRotamer populationsMethyl carbonFast exchangeSide-chain rotamersJ-couplingsTransmembrane peptidesDimer interfaceRotameric statesProtein systemsRotamersShift distributionGlycophorin A.DimersChainMethylFourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban
Ludlam C, Arkin I, Liu X, Rothman M, Rath P, Aimoto S, Smith S, Engelman D, Rothschild K. Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban. Biophysical Journal 1996, 70: 1728-1736. PMID: 8785331, PMCID: PMC1225141, DOI: 10.1016/s0006-3495(96)79735-7.Peer-Reviewed Original ResearchConceptsSite-directed isotope labelingLocal secondary structureIsotope labelingSecondary structureSelective ion channelsTotal reflection Fourier transformPeptide amide groupsAmide IReflection Fourier transformDeuterium/hydrogen exchangeTransmembrane domainMembrane domainsMembrane proteinsTransmembrane orientationAmino acid fragmentSpectroscopic characterizationIon channelsHydrophobic regionAmide carbonylProtein backboneCardiac muscle cellsAmide groupLipid bilayersATPase activityFourier transform