Koehler, Joerg and Erlach, Markus Beck and Crusca, Edson and Kremer, Werner and Munte, Claudia E. and Kalbitzer, Hans Robert (2012) Pressure Dependence of N-15 Chemical Shifts in Model Peptides Ac-Gly-Gly-X-Ala-NH2. MATERIALS, 5 (10). pp. 1774-1786. ISSN 1996-1944,
Full text not available from this repository. (Request a copy)Abstract
High pressure NMR spectroscopy has developed into an important tool for studying conformational equilibria of proteins in solution. We have studied the amide proton and nitrogen chemical shifts of the 20 canonical amino acids X in the random-coil model peptide Ac-Gly-Gly-X-Ala-NH2, in a pressure range from 0.1 to 200 MPa, at a proton resonance frequency of 800 MHz. The obtained data allowed the determination of first and second order pressure coefficients with high accuracy at 283 K and pH 6.7. The mean first and second order pressure coefficients <B-1(15N)> and <B-2(15N)> for nitrogen are 2.91 ppm/GPa and -2.32 ppm/GPa(2), respectively. The corresponding values <B-1(1H)> and <B-2(1H)> for the amide protons are 0.52 ppm/GPa and -0.41 ppm/GPa(2). Residual dependent (1)J(1H15N)-coupling constants are shown.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | H-1-NMR PARAMETERS; AQUEOUS-SOLUTIONS; NMR-SPECTROSCOPY; PROTEINS; ASSIGNMENT; STATES; CELL; ALA; tetrapeptide; high pressure; NMR spectroscopy; random-coil; chemical shift; J-coupling; nitrogen; amide group, backbone |
| 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: | 05 May 2020 08:41 |
| Last Modified: | 05 May 2020 08:41 |
| URI: | https://pred.uni-regensburg.de/id/eprint/18007 |
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