A Biophysical Study of Integral Membrane Protein Folding †
Hunt J, Earnest T, Bousché O, Kalghatgi K, Reilly K, Horváth C, Rothschild K, Engelman D. A Biophysical Study of Integral Membrane Protein Folding †. Biochemistry 1997, 36: 15156-15176. PMID: 9398244, DOI: 10.1021/bi970146j.Peer-Reviewed Original ResearchConceptsAlpha-helical integral membrane proteinsIntegral membrane proteinsMembrane proteinsIntegral membrane protein foldingMembrane protein foldingNon-native conformationsStable secondary structureCellular chaperonesBiophysical dissectionBeta-sheet structureProtein foldingIndividual polypeptidesBiophysical studiesStructure of bacteriorhodopsinTertiary structureSecondary structureReconstitution protocolsG helicesPolypeptideF helixProteinPhospholipid vesiclesHelixFoldingBacteriorhodopsinAssessment of the aggregation state of integral membrane proteins in reconstituted phospholipid vesicles using small angle neutron scattering11Edited by M. F. Moody
Hunt J, McCrea P, Zaccaı̈ G, Engelman D. Assessment of the aggregation state of integral membrane proteins in reconstituted phospholipid vesicles using small angle neutron scattering11Edited by M. F. Moody. Journal Of Molecular Biology 1997, 273: 1004-1019. PMID: 9367787, DOI: 10.1006/jmbi.1997.1330.Peer-Reviewed Original ResearchConceptsMembrane protein complexesIntegral membrane proteinsProtein complexesMembrane proteinsIntegral membrane protein complexPhospholipid vesiclesSmall unilamellar phospholipid vesiclesUnilamellar phospholipid vesiclesMolecular massF. MoodySpatial arrangementNon-ionic detergentIndividual complexesVesiclesModel systemMonomeric bacteriorhodopsinProteinUnknown scopeComplexesAggregation stateRadius of gyrationBacteriorhodopsinDetergentsBilayers