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Probing structure and dynamics of protein assemblies by magic angle spinning NMR spectroscopy
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scholarly article
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title
Probing structure and dynamics of protein assemblies by magic angle spinning NMR spectroscopy
(English)
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stated in
PubMed
main subject
protein structure
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spectroscopy
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NMR spectroscopy
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author name string
Si Yan
series ordinal
1
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Crossref
Christopher L. Suiter
series ordinal
2
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Crossref
Guangjin Hou
series ordinal
3
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Crossref
Huilan Zhang
series ordinal
4
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Tatyana Polenova
series ordinal
5
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language of work or name
English
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PubMed
publication date
17 September 2013
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published in
Accounts of Chemical Research
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PubMed
volume
46
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PubMed
issue
9
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PubMed
page(s)
2047-58
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cites work
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Resonance Assignments and Secondary Structure Analysis of Dynein Light Chain 8 by Magic Angle Spinning NMR Spectroscopy
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1H-13C/1H-15N heteronuclear dipolar recoupling by R-symmetry sequences under fast magic angle spinning for dynamics analysis of biological and organic solids
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Dynamics of reassembled thioredoxin studied by magic angle spinning NMR: snapshots from different time scales
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Rapid three-dimensional MAS NMR spectroscopy at critical sensitivity
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Large protein complexes with extreme rotational correlation times investigated in solution by magic-angle-spinning NMR spectroscopy
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Magic angle spinning NMR spectroscopy of thioredoxin reassemblies.
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Proton-detected solid-state NMR spectroscopy of fully protonated proteins at 40 kHz magic-angle spinning
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Filamentous phage studied by magic-angle spinning NMR: resonance assignment and secondary structure of the coat protein in Pf1
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Constant-time through-bond 13C correlation spectroscopy for assigning protein resonances with solid-state NMR spectroscopy
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Low-power high-resolution solid-state NMR of peptides and proteins
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Long-range structural restraints in spin-labeled proteins probed by solid-state nuclear magnetic resonance spectroscopy
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retrieved
12 December 2020
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Identifiers
DOI
10.1021/AR300309S
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3051424
OpenCitations bibliographic resource ID
3051424
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3051424
PMCID
3748245
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3051424
PubMed ID
23402263
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3051424
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