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1H-nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH

✍ Scribed by Arno Bundi; Kurt Wüthrich

Book ID
102762886
Publisher
Wiley (John Wiley & Sons)
Year
1979
Tongue
English
Weight
615 KB
Volume
18
Category
Article
ISSN
0006-3525

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1H-nmr parameters of the common amino ac
1H-nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
✍ Arno Bundi; Kurt Wüthrich 📂 Article 📅 1979 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 615 KB

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

Carbon-13 NMR chemical shifts of the com
Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly- X-L- Ala-OH
✍ René Richarz; Kurt Wüthrich 📂 Article 📅 1978 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 483 KB 👁 1 views

## 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