2001
Helical membrane proteins: diversity of functions in the context of simple architecture
Ubarretxena-Belandia I, Engelman D. Helical membrane proteins: diversity of functions in the context of simple architecture. Current Opinion In Structural Biology 2001, 11: 370-376. PMID: 11406389, DOI: 10.1016/s0959-440x(00)00217-7.Peer-Reviewed Original ResearchConceptsHelical membrane proteinsGenome-wide scaleAlpha-helical conformationDiversity of functionsIdentification of motifsMembrane proteinsProtein regionsHelix interactionsPolar sidechainsStructural roleLipid bilayersProteinDiversityMotifUse of deviationsConformationSidechainsFunctionFurther investigationBilayersSequestrationIdentification
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