A study of the NH NMR signals of Gly-Gly-X-Ala tetrapeptides in H2O at low temperature.
β Scribed by M.A. Jimenez; J.L. Nieto; M. Rico; J. Santoro; J. Herranz; F.J. Bermejo
- Book ID
- 107802887
- Publisher
- Elsevier Science
- Year
- 1986
- Tongue
- English
- Weight
- 222 KB
- Volume
- 143
- Category
- Article
- ISSN
- 0022-2860
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The 'H-nmr chemical shifts and the spin-spin coupling constants of the common amino acid residues were measured in solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH in D2O and H20, and the influence of X on the nmr parameters of the neighboring residues Gly 2 and Ala 4 was investigated. The
## Abstract The ^13^C nmr chemical shifts of the common amino acid residues were measured in D~2~O solutions of the linear tetrapeptides HβGlyβGlyβXβLβAlaβOH. 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