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
Tertiary structure of bacteriorhodopsin Positions and orientations of helices A and B in the structural map determined by neutron diffraction
Popot J, Engelman D, Gurel O, Zaccaï G. Tertiary structure of bacteriorhodopsin Positions and orientations of helices A and B in the structural map determined by neutron diffraction. Journal Of Molecular Biology 1989, 210: 829-847. PMID: 2614846, DOI: 10.1016/0022-2836(89)90111-3.Peer-Reviewed Original Research