Mass Spectrometry-From Peripheral Proteins to Membrane Motors

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dc.contributor.authorMorgner, Nina
dc.contributor.authorMontenegro, Felipe
dc.contributor.authorBarrera, Nelson P.
dc.contributor.authorRobinson, Carol V.
dc.date.accessioned2024-01-10T13:14:38Z
dc.date.available2024-01-10T13:14:38Z
dc.date.issued2012
dc.description.abstractThat membrane protein complexes could survive in the gas phase had always seemed impossible. The lack of chargeable residues, high hydrophobicity, and poor solubility and the vast excess of detergent contributed to the view that it would not be possible to obtain mass spectra of intact membrane complexes. With the recent success in recording mass spectra of these complexes, first from recombinant sources and later from the cellular environment, many surprising properties of these gas phase membrane complexes have been revealed. The first of these was that the interactions between membrane and soluble subunits could survive in vacuum, without detergent molecules adhering to the complex. The second unexpected feature was that their hydrophobicity and, consequently, lower charge state did not preclude ionization. The final surprising finding was that these gas phase membrane complexes carry with them lipids, bound specifically in subunit interfaces. This provides us with an opportunity to distinguish annular lipids that surround the membrane complexes, from structural lipids that have a role in maintaining structure and subunit interactions. In this perspective, we track these developments and suggest explanations for the various discoveries made during this research. (c) 2012 Elsevier Ltd. All rights reserved.
dc.description.funderEuropean Union Council's Seventh Framework PROSPECTS (a European Research Council advanced grant)
dc.description.funderRoyal Society Professorship
dc.description.funderWellcome Trust Programme
dc.description.funderFondo Nacional de Desarrollo Cientifico y Tecnologico
dc.description.funderMillennium Nucleus
dc.description.funderMedical Research Council
dc.fechaingreso.objetodigital27-03-2024
dc.format.extent13 páginas
dc.fuente.origenWOS
dc.identifier.doi10.1016/j.jmb.2012.06.033
dc.identifier.eissn1089-8638
dc.identifier.issn0022-2836
dc.identifier.pubmedidMEDLINE:22750574
dc.identifier.urihttps://doi.org/10.1016/j.jmb.2012.06.033
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/78427
dc.identifier.wosidWOS:000309431600001
dc.information.autorucCiencias Biológicas;Barrera N;S/I;4086
dc.information.autorucCiencias Biológicas;Montenegro F ;S/I;219665
dc.issue.numero1
dc.language.isoen
dc.nota.accesocontenido parcial
dc.pagina.final13
dc.pagina.inicio1
dc.publisherACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
dc.revistaJOURNAL OF MOLECULAR BIOLOGY
dc.rightsacceso restringido
dc.subjectmembrane protein complexes
dc.subjectmass spectrometry
dc.subjectdetergent micelles
dc.subjectELECTROSPRAY-IONIZATION
dc.subject3-DIMENSIONAL STRUCTURE
dc.subjectTRANSMEMBRANE PEPTIDE
dc.subjectABC TRANSPORTER
dc.subjectATP SYNTHASE
dc.subjectK+ CHANNEL
dc.subjectGAS-PHASE
dc.subjectCOMPLEXES
dc.subjectBINDING
dc.subjectSTOICHIOMETRY
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleMass Spectrometry-From Peripheral Proteins to Membrane Motors
dc.typeartículo
dc.volumen423
sipa.codpersvinculados4086
sipa.codpersvinculados219665
sipa.indexWOS
sipa.indexScopus
sipa.trazabilidadCarga SIPA;09-01-2024
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