NMR techniques for very large proteins and rnas in solution

dc.contributor.authorTzakos, A. G.en
dc.contributor.authorGrace, C. R.en
dc.contributor.authorLukavsky, P. J.en
dc.contributor.authorRiek, R.en
dc.date.accessioned2015-11-24T16:42:47Z
dc.date.available2015-11-24T16:42:47Z
dc.identifier.issn1056-8700-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8596
dc.rightsDefault Licence-
dc.subject*Algorithmsen
dc.subjectComplex Mixtures/analysis/chemistryen
dc.subjectComputer Simulationen
dc.subjectMacromolecular Substances/chemistryen
dc.subjectMagnetic Resonance Spectroscopy/*methodsen
dc.subject*Models, Chemicalen
dc.subject*Models, Molecularen
dc.subjectMolecular Conformationen
dc.subjectProteins/analysis/*chemistryen
dc.subjectRNA/analysis/*chemistryen
dc.subjectSequence Analysis/*methodsen
dc.subjectSolutionsen
dc.titleNMR techniques for very large proteins and rnas in solutionen
heal.abstractThree-dimensional structure determination of small proteins and oligonucleotides by solution NMR is established. With the development of novel NMR and labeling techniques, structure determination is now feasible for proteins with a molecular mass of up to approximately 100 kDa and RNAs of up to 35 kDa. Beyond these molecular masses special techniques and approaches are required for applying NMR as a multiprobe method for structural investigations of proteins and RNAs. It is the aim of this review to summarize the NMR techniques and approaches available to advance the molecular mass limit of NMR both for proteins (up to 1 MDa) and RNAs (up to 100 kDa). Physical pictures of the novel techniques, their experimental applications, as well as labeling and assignment strategies are discussed and accompanied by future perspectives.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primary10.1146/annurev.biophys.35.040405.102034-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/16689639-
heal.identifier.secondaryhttp://www.annualreviews.org/doi/abs/10.1146/annurev.biophys.35.040405.102034-
heal.journalNameAnnu Rev Biophys Biomol Structen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2006-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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