Erlach, Markus Beck and Koehler, Joerg and Crusca, Edson and Munte, Claudia E. and Kainosho, Masatsune and Kremer, Werner and Kalbitzer, Hans Robert (2017) Pressure dependence of side chain C-13 chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH2. JOURNAL OF BIOMOLECULAR NMR, 69 (2). pp. 53-67. ISSN 0925-2738, 1573-5001
Full text not available from this repository. (Request a copy)Abstract
For evaluating the pressure responses of folded as well as intrinsically unfolded proteins detectable by NMR spectroscopy the availability of data from well-defined model systems is indispensable. In this work we report the pressure dependence of C-13 chemical shifts of the side chain atoms 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 a number of nuclei have a nonlinear dependence on pressure in the range from 0.1 to 200 MPa. The size of the polynomial pressure coefficients B (1) and B (2) is dependent on the type of atom and amino acid studied. For H-N, N and C-alpha the first order pressure coefficient B (1) is also correlated to the chemical shift at atmospheric pressure. The first and second order pressure coefficients of a given type of carbon atom 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 also are weakly correlated. The downfield shifts of the methyl resonances suggest that gauche conformers of the side chains are not preferred with pressure. The valine and leucine methyl groups in the model peptides were assigned using stereospecifically C-13 enriched amino acids with the pro-R carbons downfield shifted relative to the pro-S carbons.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | NUCLEAR-MAGNETIC-RESONANCE; PROTEIN SECONDARY STRUCTURE; PANCREATIC TRYPSIN-INHIBITOR; RANDOM COIL H-1; GLY-X-ALA; NMR-SPECTROSCOPY; AMINO-ACIDS; AQUEOUS-SOLUTIONS; HYDROSTATIC-PRESSURE; H-1-NMR PARAMETERS; Biosynthetically labeled; High pressure NMR; Pressure coefficients; Random coil peptides; Stereospecific assignment; C-13 shifts |
| 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: | 14 Dec 2018 13:19 |
| Last Modified: | 19 Feb 2019 08:16 |
| URI: | https://pred.uni-regensburg.de/id/eprint/2089 |
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