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Assignment of proton and carbon NMR signals of didemnin A in solution
Author(s) -
Kessler H.,
Will M.,
Sheldrick G. M.,
Antel J.
Publication year - 1988
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260260613
Subject(s) - heteronuclear molecule , chemistry , pulse sequence , two dimensional nuclear magnetic resonance spectroscopy , heteronuclear single quantum coherence spectroscopy , inverse , spectral line , proton , coherence (philosophical gambling strategy) , proton nmr , nuclear magnetic resonance spectroscopy , analytical chemistry (journal) , nuclear magnetic resonance , stereochemistry , organic chemistry , physics , quantum mechanics , geometry , mathematics
Several one‐ and two‐dimensional techniques have been used to assign the 1 H and 13 C NMR spectra of the cyclic heptadepsipeptide didemnin A in DMSO. The composition and sequence of the amino acid residues was known beforehand and could be confirmed by heteronuclear proton–carbon long‐range couplings using the COLOC experiment and a recently proposed new inverse technique using Gaussian‐shaped pulses. The aliphatic methyl resonances of the isostatin, hydroxyisovalerylpropionyl, N ‐methylleucine and leucine residues were assigned by means of the TOCSY and NOESY techniques. Aliphatic carbon assignment was performed by inverse correlation via heteronuclear double quantum coherence.

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