The assignment of nonexchanging protons of a small microcrystalline protein, the alpha-spectrin SH3 domain (7.2 kDa, 62 residues), was achieved by means of three-dimensional (3D) heteronuclear (1H-13C-13C) magic-angle spinning (MAS) NMR dipolar correlation spectroscopy. With the favorable combinatio
A two-dimensional NMR strategy for the complete 1H chemical shift assignment of extended proton spin systems in triterpenoids
✍ Scribed by Duraikkannu Loganathan; Girish K. Trivedi; K. V. R. Chary
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 505 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0749-1581
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✦ Synopsis
Abstract
An assignment strategy that utilizes one‐dimensional lanthanide‐induced methyl proton shifts, reported ^13^C NMR data of model compounds and two‐dimensional ^1^H and ^13^C shift correlated spectroscopy, homonuclear proton chemical shift correlated spectroscopy and nuclear Overhauser enhancement spectroscopy methods was demonstrated to be effective for the complete ^1^H chemical shift assignments of extended proton spin‐systems in a triterpenoid viz., 3‐keto‐urs‐12‐en‐24‐oic acid methyl ester. Complete ^13^C chemical shift assignments have also been accomplished.
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