2014
Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry
Sriswasdi S, Harper SL, Tang HY, Gallagher PG, Speicher DW. Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 1801-1806. PMID: 24453214, PMCID: PMC3918770, DOI: 10.1073/pnas.1317620111.Peer-Reviewed Original ResearchConceptsMass spectrometryConformational changesStructural mass spectrometryLarge conformational rearrangementsCell membraneMembrane integrityMass spectrometry characterizationRed cell spectrinUnidentified mechanistic insightCell membrane integrityProtein complexesMacromolecular complexesDiverse functionsCell shapeBiological processesFlexible proteinsConformational rearrangementsDimer-tetramer equilibriumRed cell membraneOpen dimersCell typesΑ-spectrinKey mechanistic roleTetramerization siteBiophysical data
2010
A Fused α-β “Mini-spectrin” Mimics the Intact Erythrocyte Spectrin Head-to-head Tetramer*
Harper SL, Li D, Maksimova Y, Gallagher PG, Speicher DW. A Fused α-β “Mini-spectrin” Mimics the Intact Erythrocyte Spectrin Head-to-head Tetramer*. Journal Of Biological Chemistry 2010, 285: 11003-11012. PMID: 20139081, PMCID: PMC2856305, DOI: 10.1074/jbc.m109.083048.Peer-Reviewed Original ResearchConceptsN-terminal regionFull-length dimerC-terminal regionRed cell membrane integrityGel filtration analysisLateral associationCell membrane integrityOligomeric stateFusion proteinAlpha-spectrinTetramer formationBeta subunitC-terminalN-terminalConformational statesFunctional studiesFiltration analysisMembrane integritySpectrin heterodimersTerminal peptidesDimer interactionsDistinct groupsSpectrinSpectrin dimersProtein