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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

Richarz, René, Wüthrich, Kurt·1978·Biopolymers

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 are compared with the corresponding 13 C chemical shifts in the protected tetrapeptides CF 3 CO‐Gly‐Gly‐X‐L‐Ala‐OCH 3, the linear pentapeptides H‐Gly‐Gly‐X‐Gly‐Gly‐OH, and the free amino acids. On this basism the selection of suitable “random coil” 13 C chemical shifts for conformational studies of polypeptides chain is discussed.

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Metadata

Authors
Richarz, R., & Wüthrich, K.
Venue
Biopolymers
Publisher
Wiley
Published
1978-09
Volume
17
Issue
9
Pages
2133-2141
ISSN
  • 0006-3525 (ISSN-L)
  • 1097-0282
OpenAlex
W2010923110
Cited by
214
References
0
FWCI
3.45
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: 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. https://app.cochat.ai/papers/10.1002/bip.1978.360170908
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Richarz, R., & Wüthrich, K. (1978). 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. Biopolymers. https://doi.org/10.1002/bip.1978.360170908

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