1999
Multistep Denaturation of Borrelia burgdorferi OspA, a Protein Containing a Single-Layer β-Sheet †
Koide S, Bu Z, Risal D, Pham T, Nakagawa T, Tamura A, Engelman D. Multistep Denaturation of Borrelia burgdorferi OspA, a Protein Containing a Single-Layer β-Sheet †. Biochemistry 1999, 38: 4757-4767. PMID: 10200164, DOI: 10.1021/bi982443+.Peer-Reviewed Original ResearchConceptsSolution small-angle X-ray scatteringChemical shift differencesSingle-layer β-sheetSignificant kinetic barrierSmall-angle X-ray scatteringHeteronuclear NMR spectroscopyDifferential scanning calorimetryNMR spectroscopyRadius of gyrationX-ray scatteringDenaturation reactionNMR measurementsShift differencesKinetic barrierRigid moleculesScanning calorimetrySAXS measurementsΒ-sheetCooperative transitionReactionLys residuesBorrelia burgdorferi OspANative proteinBeta-sheet segmentThermal denaturation reaction
1991
Small-angle X-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker region retains a predominantly alpha-helical conformation.
Kataoka M, Head J, Persechini A, Kretsinger R, Engelman D. Small-angle X-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker region retains a predominantly alpha-helical conformation. Biochemistry 1991, 30: 1188-92. PMID: 1991098, DOI: 10.1021/bi00219a004.Peer-Reviewed Original ResearchConceptsLinker regionCentral helixCalcium-dependent conformational changeWild-type proteinCentral linker regionSmall-angle X-rayAlpha-helical conformationGlu-84Calmodulin mutantsMutant formsGlu-83Wild typeMutantsNative proteinConformational changesCalmodulinProteinSer-81DeletionPresence of Ca2Binding of melittinSignificant size changesGlobular conformationRadius of gyrationHelix
1988
Bacteriorhodopsin in and out of Shape: Experimental Evidence in Favor of a Two-Stage Mechanism for Integral Membrane Protein Folding
Popot J, Engelman D. Bacteriorhodopsin in and out of Shape: Experimental Evidence in Favor of a Two-Stage Mechanism for Integral Membrane Protein Folding. Jerusalem Symposia 1988, 21: 381-398. DOI: 10.1007/978-94-009-3075-9_25.Peer-Reviewed Original ResearchIntegral membrane proteinsMembrane proteinsHelical integral membrane proteinsIntegral membrane protein foldingIntegral membrane protein bacteriorhodopsinMembrane protein foldingTransmembrane α-helicesMembrane protein bacteriorhodopsinTransmembrane helicesProtein foldingRenaturation experimentsVesicle fusionExtensive rearrangementNative proteinPolypeptide chainΑ-helixSequence segmentsLipid vesiclesProtein bacteriorhodopsinProteolytic fragmentsProteinFoldingHelixLipid phaseBacteriorhodopsin