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