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 and for nitrogen are 2.91 ppm/GPa and −2.32 ppm/GPa2, respectively. The corresponding values and for the amide protons are 0.52 ppm/GPa and −0.41 ppm/GPa2. Residual dependent 1J1H15N-coupling constants are shown.
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Koehler, J.; Beck Erlach, M.; Crusca, E.; Kremer, W.; Munte, C.E.; Kalbitzer, H.R. Pressure Dependence of 15N Chemical Shifts in Model Peptides Ac-Gly-Gly-X-Ala-NH2. Materials 2012, 5, 1774-1786.
Koehler J, Beck Erlach M, Crusca E, Kremer W, Munte CE, Kalbitzer HR. Pressure Dependence of 15N Chemical Shifts in Model Peptides Ac-Gly-Gly-X-Ala-NH2. Materials. 2012; 5(10):1774-1786.
Koehler, Joerg; Beck Erlach, Markus; Crusca, Edson; Kremer, Werner; Munte, Claudia E.; Kalbitzer, Hans Robert. 2012. "Pressure Dependence of 15N Chemical Shifts in Model Peptides Ac-Gly-Gly-X-Ala-NH2." Materials 5, no. 10: 1774-1786.