1992
Truncated staphylococcal nuclease is compact but disordered.
Flanagan J, Kataoka M, Shortle D, Engelman D. Truncated staphylococcal nuclease is compact but disordered. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 748-752. PMID: 1731350, PMCID: PMC48316, DOI: 10.1073/pnas.89.2.748.Peer-Reviewed Original ResearchConceptsComplete folding pathwayWild-type levelsCarboxyl-terminal deletionsSecondary structural featuresNative-like conformationPersistent secondary structureProtein foldsCarboxyl terminusFolding pathwaysPolypeptide chainSecondary structureAmino acidsStaphylococcal nucleaseSmall-angle X-rayNuclear magnetic resonanceCircular dichroismPhysiological conditionsNucleasePotent inhibitorDeletionSolvent exclusionMolecules resultsStructural featuresPresence of calciumRibosomes
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