Protein resonance assignment by solid-state NMR based on 1 H-detected 13 C double-quantum spectrosco...
Protein resonance assignment by solid-state NMR based on 1 H-detected 13 C double-quantum spectroscopy at fast MAS
About this item
Full title
Author / Creator
Publisher
Netherlands
Journal title
Language
English
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Publication information
Publisher
Netherlands
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More information
Scope and Contents
Contents
Solid-state NMR spectroscopy is a powerful technique to study insoluble and non-crystalline proteins and protein complexes at atomic resolution. The development of proton (
H) detection at fast magic-angle spinning (MAS) has considerably increased the analytical capabilities of the technique, enabling the acquisition of
H-detected fingerprint...
Alternative Titles
Full title
Protein resonance assignment by solid-state NMR based on 1 H-detected 13 C double-quantum spectroscopy at fast MAS
Authors, Artists and Contributors
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Record Identifier
TN_cdi_pubmed_primary_34813018
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_34813018
Other Identifiers
E-ISSN
1573-5001
DOI
10.1007/s10858-021-00386-6
