In-Cell NMR Spectroscopy: Biomolecular Structure and Function
dc.contributor.author | Burz, David S. | * |
dc.contributor.author | Shekhtman, Alexander | * |
dc.date.accessioned | 2021-02-11T16:03:38Z | |
dc.date.available | 2021-02-11T16:03:38Z | |
dc.date.issued | 2020 | * |
dc.date.submitted | 2020-06-09 16:38:57 | * |
dc.identifier | 46063 | * |
dc.identifier.uri | https://directory.doabooks.org/handle/20.500.12854/50093 | |
dc.description.abstract | This 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.language | English | * |
dc.subject | QH301-705.5 | * |
dc.subject | Q1-390 | * |
dc.subject.classification | thema EDItEUR::P Mathematics and Science::PS Biology, life sciences | en_US |
dc.subject.other | protein NMR | * |
dc.subject.other | time-resolved NMR | * |
dc.subject.other | Ribosome | * |
dc.subject.other | structural calculation 4 | * |
dc.subject.other | crystalline and amorphous starch | * |
dc.subject.other | in-cell NMR | * |
dc.subject.other | protein dynamics | * |
dc.subject.other | DNP | * |
dc.subject.other | protein modification | * |
dc.subject.other | Tau | * |
dc.subject.other | spectrum reconstruction 3 | * |
dc.subject.other | mRNA | * |
dc.subject.other | Thioredoxin | * |
dc.subject.other | protein structure | * |
dc.subject.other | protein interactions | * |
dc.subject.other | drug discovery | * |
dc.subject.other | protein structure determination 1 | * |
dc.subject.other | review | * |
dc.subject.other | enzyme activity | * |
dc.subject.other | MARK2 phosphorylation | * |
dc.subject.other | post-translational modifications | * |
dc.subject.other | Dihydrofolate reductase | * |
dc.subject.other | mammalian cells | * |
dc.subject.other | target engagement | * |
dc.subject.other | non-uniform sampling 2 | * |
dc.subject.other | paramagnetic effects | * |
dc.subject.other | protein structure-function | * |
dc.subject.other | cross-correlated relaxation | * |
dc.subject.other | structure function | * |
dc.subject.other | rRNA | * |
dc.subject.other | 2D INADEQUATE | * |
dc.subject.other | lipid membrane | * |
dc.subject.other | Thymidylate synthase | * |
dc.subject.other | whole cell NMR | * |
dc.subject.other | enzyme kinetics | * |
dc.subject.other | magic-angle spinning | * |
dc.subject.other | live cell | * |
dc.subject.other | solid-state NMR | * |
dc.subject.other | Adenylate kinase | * |
dc.subject.other | DNA | * |
dc.subject.other | in-situ NMR | * |
dc.subject.other | antimicrobial peptide | * |
dc.subject.other | NMR spectroscopy | * |
dc.subject.other | intrinsically disordered proteins | * |
dc.title | In-Cell NMR Spectroscopy: Biomolecular Structure and Function | * |
dc.type | book | |
oapen.identifier.doi | 10.3390/books978-3-03928-255-5 | * |
oapen.relation.isPublishedBy | 46cabcaa-dd94-4bfe-87b4-55023c1b36d0 | * |
oapen.relation.isbn | 9783039282555 | * |
oapen.relation.isbn | 9783039282548 | * |
oapen.pages | 152 | * |
oapen.edition | 1st | * |
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