Quantitative single-molecule imaging of protein assembly in membranes

DC FieldValueLanguage
dc.contributor.authorJenner, A.
dc.contributor.authorShalaby, R.
dc.contributor.authorCosentino, K.
dc.contributor.editorIglic
dc.contributor.editorRappolt
dc.contributor.editorGarcia-SAez
dc.date.accessioned2021-12-23T16:35:19Z-
dc.date.available2021-12-23T16:35:19Z-
dc.date.issued2020
dc.identifier.isbn9780128209677
dc.identifier.issn24519634
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/18427-
dc.description.abstractAccurate knowledge of the mechanisms of assembly of protein complexes is essential to understand their structure and control their function. Deep insight into these mechanisms requires information at the single-molecule level to unveil processes which would be masked by ensemble measurements. Here, we describe single-molecule imaging (SMI) as a powerful tool to provide a quantitative characterization of the assembly of protein complexes through the determination of their copy number (or stoichiometry). We focus on membrane protein complexes and describe experimental and analytical strategies for their stoichiometry characterization in both model and cellular membranes. © 2020 Elsevier Inc.
dc.language.isoen
dc.publisherElsevier B.V.
dc.relation.ispartofAdvances in Biomembranes and Lipid Self-Assembly
dc.subjectMembrane protein assembly
dc.subjectPhoton counting confocal microscopy
dc.subjectProtein fluorophores
dc.subjectProtein oligomers
dc.subjectSingle-molecule imaging
dc.subjectStoichiometry analysis
dc.subjectTIRF microscopy
dc.titleQuantitative single-molecule imaging of protein assembly in membranes
dc.typejournal article
dc.identifier.doi10.1016/bs.abl.2020.02.004
dc.identifier.scopus2-s2.0-85082521284
dc.identifier.urlhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85082521284&doi=10.1016%2fbs.abl.2020.02.004&partnerID=40&md5=e711c10c3d6942a1fc6000328ee7f0aa
dc.description.volume31
dc.description.startpage81
dc.description.endpage128
dcterms.isPartOf.abbreviationAdv. Biomembr. Lipid Self-Assembly
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidCoKa893-
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