Erlach, Markus Beck and Koehler, Joerg and Crusca, Edson and Kremer, Werner and Munte, Claudia E. and Kalbitzer, Hans Robert (2016) Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH2. JOURNAL OF BIOMOLECULAR NMR, 65 (2). pp. 65-77. ISSN 0925-2738, 1573-5001
Full text not available from this repository. (Request a copy)Abstract
For a better understanding of nuclear magnetic resonance (NMR) detected pressure responses of folded as well as unstructured proteins the availability of data from well-defined model systems are indispensable. In this work we report the pressure dependence of chemical shifts of the backbone atoms H-1(alpha), C-13(alpha) and C-13' in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (Xxx one of the 20 canonical amino acids). Contrary to expectation the chemical shifts of these nuclei have a nonlinear dependence on pressure in the range from 0.1 to 200 MPa. The polynomial pressure coefficients B (1) and B (2) are dependent on the type of amino acid studied. The coefficients of a given nucleus show significant linear correlations suggesting that the NMR observable pressure effects in the different amino acids have at least partly the same physical cause. In line with this observation the magnitude of the second order coefficients of nuclei being direct neighbors in the chemical structure are also weakly correlated.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PROTEIN SECONDARY STRUCTURE; MAGNETIC-RESONANCE SPECTRA; RANDOM COIL H-1; GLY-X-ALA; AQUEOUS-SOLUTIONS; NMR-SPECTROSCOPY; HYDROGEN-BONDS; AMINO-ACIDS; HYDROSTATIC-PRESSURE; H-1-NMR PARAMETERS; NMR; High pressure; Peptide; Random coil |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 22 Mar 2019 09:25 |
| Last Modified: | 22 Mar 2019 09:25 |
| URI: | https://pred.uni-regensburg.de/id/eprint/2828 |
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