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 calciumRibosomesDimerization of Glycophorin a Transmembrane Helices: Mutagenesis and Modeling
Engelman D, Adair B, Brünger A, Flanagan J, Lemmon M, Treutlein H, Zhang J. Dimerization of Glycophorin a Transmembrane Helices: Mutagenesis and Modeling. Jerusalem Symposia 1992, 25: 115-125. DOI: 10.1007/978-94-011-2718-9_11.Peer-Reviewed Original ResearchTransmembrane domainSingle transmembrane domainSite-specific mutagenesisGpA dimerTransmembrane helicesDeletion mutagenesisTransmembrane portionCarboxy terminusDimer interfaceHanded supercoilMutagenesisChimera formLipid bilayersGlycophorin AStaphylococcal nucleaseHuman erythrocyte sialoglycoproteinSDS-PAGEErythrocyte sialoglycoproteinDimerizationClose associationDomainDimersSupercoilsNucleaseTerminus