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
1979
Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase.
Pickover C, McKay D, Engelman D, Steitz T. Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase. Journal Of Biological Chemistry 1979, 254: 11323-11329. PMID: 387770, DOI: 10.1016/s0021-9258(19)86488-8.Peer-Reviewed Original ResearchConceptsYeast phosphoglycerate kinasePhosphoglycerate kinaseConformational changesTernary complexSubstrate bindingHinge motionKinaseSubstrate MgATPCleft closureSmall-angle X-raySeparate bindingRadius of gyrationAngle X-rayMgATPBindingApparent similarityComplexesCleftEnzymeObserved changesHexokinaseGyration decreasesDomainSimilarity
1971
Structural comparisons of native and reaggregated membranes.
Engelman D, Metcalfe J, Metcalfe S. Structural comparisons of native and reaggregated membranes. British Journal Of Pharmacology 1971, 41: 382p. PMID: 5572285, PMCID: PMC1703325.Peer-Reviewed Original Research
1968
Characterization of the plasma membrane of Mycoplasma laidlawii. IV. Structure and composition of membrane and aggregated components
Engelman D, Morowitz H. Characterization of the plasma membrane of Mycoplasma laidlawii. IV. Structure and composition of membrane and aggregated components. Biochimica Et Biophysica Acta 1968, 150: 385-396. PMID: 5650391, DOI: 10.1016/0005-2736(68)90137-5.Peer-Reviewed Original ResearchCharacterization of the plasma membrane of Mycoplasma laidlawii. III. The formation and aggregation of small lipoprotein structures derived from sodium dodecyl sulfate-solubilized membrane components
Engelman D, Morowitz H. Characterization of the plasma membrane of Mycoplasma laidlawii. III. The formation and aggregation of small lipoprotein structures derived from sodium dodecyl sulfate-solubilized membrane components. Biochimica Et Biophysica Acta 1968, 150: 376-384. PMID: 5650390, DOI: 10.1016/0005-2736(68)90136-3.Peer-Reviewed Original ResearchConceptsMembrane componentsSucrose density gradient centrifugationPlasma membraneSame proteinMycoplasma laidlawiiAnalytical ultracentrifugationDensity gradient centrifugationBuoyant densityGradient centrifugationProteinLipoprotein structureProtein ratioDivalent cationsLipoprotein aggregatesMembraneLarge aggregatesM Mg2LaidlawiiAggregatesLipidsUltracentrifugationSingle peak
1967
Characterization of the plasma membrane of Mycoplasma laidlawii. II. Modes of aggregation of solubilized membrane components
Terry T, Engelman D, Morowitz H. Characterization of the plasma membrane of Mycoplasma laidlawii. II. Modes of aggregation of solubilized membrane components. Biochimica Et Biophysica Acta 1967, 135: 391-405. PMID: 6058126, DOI: 10.1016/0005-2736(67)90029-6.Peer-Reviewed Original Research