A solid state NMR technique for the determination of peptide backbone conformations at specific sites in unoriented samples under magic angle spinning (MAS) is described and demonstrated on a doubly labeled polycrystalline sample of the tripeptide AlaGlyGly and a sextuply labeled lyophilized sample
✦ LIBER ✦
Carbon-13 Chemical Shift Tensors in meso-Erythritol, Measuring OH Dihedral Angles
✍ Scribed by Liu, Fang; Phung, Cu G.; Alderman, D. W.; Grant, David M.
- Book ID
- 126882471
- Publisher
- American Chemical Society
- Year
- 1995
- Tongue
- English
- Weight
- 642 KB
- Volume
- 117
- Category
- Article
- ISSN
- 0002-7863
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## Abstract The ^13^C nmr chemical shifts of the common amino acid residues were measured in D~2~O solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OH. For Asp, Glu, Lys, Tyr and His, the titration shifts arising from the ionization of te amino acid side chains were also obtained. These data