2000
A view of dynamics changes in the molten globule-native folding step by quasielastic neutron scattering11Edited by P. E. Wright
Bu Z, Neumann D, Lee S, Brown C, Engelman D, Han C. A view of dynamics changes in the molten globule-native folding step by quasielastic neutron scattering11Edited by P. E. Wright. Journal Of Molecular Biology 2000, 301: 525-536. PMID: 10926525, DOI: 10.1006/jmbi.2000.3978.Peer-Reviewed Original ResearchConceptsVibrational motionDiffusive motionPicosecond time scaleQuasielastic neutron scatteringSuch collective motionLength scalesPotential barrierQuasielastic scattering intensityCorrelation lengthJump motionShort length scalesBovine alpha-lactalbuminNeutron scatteringMolten globuleScattering intensityLong length scalesCollective motionMean-square amplitudesAtom clustersHigh-frequency motionsMolten globule stateNon-exchangeable protonsCluster sizeFrequency motionsProtein dynamics
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
1989
Melittin binding causes a large calcium-dependent conformational change in calmodulin.
Kataoka M, Head J, Seaton B, Engelman D. Melittin binding causes a large calcium-dependent conformational change in calmodulin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1989, 86: 6944-6948. PMID: 2780551, PMCID: PMC297967, DOI: 10.1073/pnas.86.18.6944.Peer-Reviewed Original ResearchConceptsConformational changesCalcium-dependent conformational changeDependent conformational changesCellular functionsTarget proteinsMelittin bindsCalmodulin functionCalmodulinSolution structureCalmodulin-melittin complexSmall-angle X-ray scatteringConformation changeAbsence of calciumCompetitive inhibitorOverall structureMelittin bindingTarget peptideMelittinPresence of calciumGlobular shapeCa2PeptidesX-ray scatteringProteinBinds
1985
Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle X-ray scattering.
Seaton B, Head J, Engelman D, Richards F. Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle X-ray scattering. Biochemistry 1985, 24: 6740-3. PMID: 4074724, DOI: 10.1021/bi00345a002.Peer-Reviewed Original Research
1984
Neutron scattering shows that cytochrome b5 penetrates deeply into the lipid bilayer
Gogol E, Engelman D. Neutron scattering shows that cytochrome b5 penetrates deeply into the lipid bilayer. Biophysical Journal 1984, 46: 491-495. PMID: 6498267, PMCID: PMC1435021, DOI: 10.1016/s0006-3495(84)84046-1.Peer-Reviewed Original Research
1983
Neutron diffraction analysis of cytochrome b5 reconstituted in deuterated lipid multilayers
Gogol E, Engelman D, Zaccai G. Neutron diffraction analysis of cytochrome b5 reconstituted in deuterated lipid multilayers. Biophysical Journal 1983, 43: 285-292. PMID: 6626669, PMCID: PMC1329297, DOI: 10.1016/s0006-3495(83)84352-5.Peer-Reviewed Original Research