Methods for study of protein dynamics and protein-protein interaction in protein-ubiquitination by electron paramagnetic resonance spectroscopy

DC FieldValueLanguage
dc.contributor.authorSteinhoff, HJ
dc.date.accessioned2021-12-23T16:03:00Z-
dc.date.available2021-12-23T16:03:00Z-
dc.date.issued2002
dc.identifier.issn10939946
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/5743-
dc.description.abstractUbiquitination is a post-translation modification whereby the C-terminal end of ubiquitin (Ub) is covalently attached to the amino group of a lysine in a target protein. Additional ubiquitin groups are added using Ub-Ub linkages to form a polyubiquitin chain. A 26S protease complex specifically binds polyubiquitinated proteins and degrades them in an ATP-dependent manner. The target lysine in the substrate protein resides in a domain that is recognized by the ubiquitination machinery in a temporally and spatially controlled manner. The accessibility and the molecular dynamics of the target domain for each protein substrate is expected to be distinctive and this article is intended to facilitate investigations in this uncharted research area of ubiquitination mediated protein turnover by means of site-directed spin labeling. Examples illustrate the methodology of electron paramagnetic resonance data acquisition and interpretation in terms of secondary and tertiary structure resolution of proteins and protein complexes. Analysis of the spin labeled side chain mobility, its solvent accessibility, the polarity of the spin label micro-environment and distances between spin labels allow to model protein domains or protein-protein interaction sites and their conformational changes with a spatial resolution at the level of the backbone fold. The structural changes accompanying protein function or protein-protein interaction can be monitored in the millisecond time range. These features make site-directed spin labeling an attractive approach for the study of protein-ubiquitin interaction and protein ubiquitination.
dc.language.isoen
dc.publisherFRONTIERS IN BIOSCIENCE INC
dc.relation.ispartofFRONTIERS IN BIOSCIENCE-LANDMARK
dc.subjectBiochemistry & Molecular Biology
dc.subjectCell Biology
dc.subjectCONFORMATIONAL-CHANGES
dc.subjectcytochrome P450
dc.subjectDISTANCE DETERMINATION
dc.subjectE-F LOOP
dc.subjectEPR
dc.subjectHIGH-FIELD EPR
dc.subjectinter-spin distance
dc.subjectINTERSPIN DISTANCES
dc.subjectLACTOSE PERMEASE
dc.subjectNITROXIDE SIDE-CHAINS
dc.subjectprotein-protein interaction
dc.subjectreview
dc.subjectsite-directed spin labeling
dc.subjectSPIN-LABELED MUTANTS
dc.subjectTIME-RESOLVED DETECTION
dc.subjectTRANSIENT MOVEMENT
dc.subjectubiquitin
dc.titleMethods for study of protein dynamics and protein-protein interaction in protein-ubiquitination by electron paramagnetic resonance spectroscopy
dc.typejournal article
dc.identifier.doi10.2741/stein
dc.identifier.isiISI:000177303000001
dc.description.volume7
dc.description.startpageC97-C110
dc.contributor.orcid0000-0002-5888-0157
dc.contributor.researcheridH-3791-2014
dc.identifier.eissn10934715
dc.publisher.place16471 SCIENTIFIC WAY, IRVINE, CA 92618 USA
dcterms.isPartOf.abbreviationFront. Biosci.
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