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dc.contributor.authorBurz, David S.*
dc.contributor.authorShekhtman, Alexander*
dc.date.accessioned2021-02-11T16:03:38Z
dc.date.available2021-02-11T16:03:38Z
dc.date.issued2020*
dc.date.submitted2020-06-09 16:38:57*
dc.identifier46063*
dc.identifier.urihttps://directory.doabooks.org/handle/20.500.12854/50093
dc.description.abstractThis Special Issue examines state-of-the-art in-cell NMR spectroscopy as it relates to biological systems of increasing complexity. The compendia of research and recent innovations from prominent laboratories in the field of solid state and solution in-cell NMR spectroscopy, metabolomics and technology development are presented. The work establishes in-cell NMR spectroscopy as the premier method for determining the structures and interaction capabilities of biological molecules at high resolution within the delicately intricate interior of living cells, and the means of utilizing cells as living laboratories to directly assess the effects of exogenous and endogenous stimuli on cell physiology.]*
dc.languageEnglish*
dc.subjectQH301-705.5*
dc.subjectQ1-390*
dc.subject.classificationthema EDItEUR::P Mathematics and Science::PS Biology, life sciencesen_US
dc.subject.otherprotein NMR*
dc.subject.othertime-resolved NMR*
dc.subject.otherRibosome*
dc.subject.otherstructural calculation 4*
dc.subject.othercrystalline and amorphous starch*
dc.subject.otherin-cell NMR*
dc.subject.otherprotein dynamics*
dc.subject.otherDNP*
dc.subject.otherprotein modification*
dc.subject.otherTau*
dc.subject.otherspectrum reconstruction 3*
dc.subject.othermRNA*
dc.subject.otherThioredoxin*
dc.subject.otherprotein structure*
dc.subject.otherprotein interactions*
dc.subject.otherdrug discovery*
dc.subject.otherprotein structure determination 1*
dc.subject.otherreview*
dc.subject.otherenzyme activity*
dc.subject.otherMARK2 phosphorylation*
dc.subject.otherpost-translational modifications*
dc.subject.otherDihydrofolate reductase*
dc.subject.othermammalian cells*
dc.subject.othertarget engagement*
dc.subject.othernon-uniform sampling 2*
dc.subject.otherparamagnetic effects*
dc.subject.otherprotein structure-function*
dc.subject.othercross-correlated relaxation*
dc.subject.otherstructure function*
dc.subject.otherrRNA*
dc.subject.other2D INADEQUATE*
dc.subject.otherlipid membrane*
dc.subject.otherThymidylate synthase*
dc.subject.otherwhole cell NMR*
dc.subject.otherenzyme kinetics*
dc.subject.othermagic-angle spinning*
dc.subject.otherlive cell*
dc.subject.othersolid-state NMR*
dc.subject.otherAdenylate kinase*
dc.subject.otherDNA*
dc.subject.otherin-situ NMR*
dc.subject.otherantimicrobial peptide*
dc.subject.otherNMR spectroscopy*
dc.subject.otherintrinsically disordered proteins*
dc.titleIn-Cell NMR Spectroscopy: Biomolecular Structure and Function*
dc.typebook
oapen.identifier.doi10.3390/books978-3-03928-255-5*
oapen.relation.isPublishedBy46cabcaa-dd94-4bfe-87b4-55023c1b36d0*
oapen.relation.isbn9783039282555*
oapen.relation.isbn9783039282548*
oapen.pages152*
oapen.edition1st*


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