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 |
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Authors: | Ren Richarz,Kurt Wü thrich |
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Affiliation: | René Richarz,Kurt Wüthrich |
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Abstract: | The 13C nmr chemical shifts of the common amino acid residues were measured in D2O 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 are compared with the corresponding 13C chemical shifts in the protected tetrapeptides CF3CO-Gly-Gly-X-L -Ala-OCH3, the linear pentapeptides H-Gly-Gly-X-Gly-Gly-OH, and the free amino acids. On this basism the selection of suitable “random coil” 13C chemical shifts for conformational studies of polypeptides chain is discussed. |
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