Conformational features and ionization states of Lys side chains in a protein studied using the ster...
Conformational features and ionization states of Lys side chains in a protein studied using the stereo-array isotope labeling (SAIL) method
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Publisher
Göttingen: Copernicus GmbH
Journal title
Language
English
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Publisher
Göttingen: Copernicus GmbH
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Scope and Contents
Contents
Although both the hydrophobic aliphatic chain and hydrophilic ζ-amino group of the Lys side chain presumably contribute to the structures and functions of proteins, the dual nature of the Lys residue has not been fully investigated using NMR spectroscopy, due to the lack of appropriate methods to acquire comprehensive information on its long consec...
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Full title
Conformational features and ionization states of Lys side chains in a protein studied using the stereo-array isotope labeling (SAIL) method
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Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_4885bc2750b04cd2b98a00f026874ded
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_4885bc2750b04cd2b98a00f026874ded
Other Identifiers
ISSN
2699-0016
E-ISSN
2699-0016
DOI
10.5194/mr-2-223-2021
