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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
Abstract
The 1 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 D 2 O and H 2 O, the influence of X on the nmr parameters of the neighboring residues Gly 2 and Ala 4 was investigated. The titration parameters for the side chains of Asp, Glu, Lys, Tyr, and His were determined. The p Ka values obtained in D 2 O, with the use of pH‐meter readings with a combination glass electrode uncorrected for istope effects, were 0.06 pH units higher in the acidic range and 0.10 pH units higher in the basic range than the corresponding p Ka values in H 2 O. This suggests that the present data are suitable “random‐coil” 1 H‐nmr parameters for conformational studies of polypeptide chains in D 2 O and H 2 O solutions.
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Cited by
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Metadata
- Authors
- Bundi, A., & Wüthrich, K.
- Venue
- Biopolymers
- Publisher
- Wiley
- Published
- 1979-02
- Volume
- 18
- Issue
- 2
- Pages
- 285-297
- ISSN
- 0006-3525 (ISSN-L)
- 1097-0282
- OpenAlex
- W2030901966
- Cited by
- 755
- References
- 0
- FWCI
- 18.91
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: 1H‐nmr parameters 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.1979.360180206
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- Bundi, A., & Wüthrich, K. (1979). 1H‐nmr parameters 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.1979.360180206
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