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Biophys Chem. 2002 May 2;96(2-3):129-40.

1H-NMR parameters of common amino acid residues measured in aqueous solutions of the linear tetrapeptides Gly-Gly-X-Ala at pressures between 0.1 and 200 MPa.

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Institut für Biophysik und physikalische Biochemie, Universität Regensburg, Regensburg, Germany.


For the interpretation of chemical shift changes induced by pressure in proteins, a comparison with random-coil data is important. For providing such a data basis, the pressure dependence of the 1H-NMR chemical shifts of the amino acids X in the random-coil model peptides Gly-Gly-X-Ala were studied for the 20 common amino acids at two pH values (pH 5.0 and 5.4) at 305 K, in the pressure range from 0.1 to 200 MPa. The largest shift changes deltadelta with pressure p can be observed for the backbone amide protons. The average linear pressure coefficient delta(deltap) is 0.38 ppm GPa(-1), with a root mean square deviation of 0.2 ppm GPa(-1). In contrast to the downfield shift typical for amide protons, the H(alpha)-resonances typically shift upfield, with a pressure coefficient of -0.025 ppm GPa(-1) and a root mean square deviation of 0.05 ppm GPa(-1). The side chain resonances are only weakly influenced by pressure, on average they are shifted by 0.014 ppm GPa(-1)) with a root mean square deviation of 0.14 ppm GPa(-1). The exceptions are the side chain amide protons of asparagine and glutamine. Here, values of 0.214 (Asn H(delta21)), 0.417 (Asn H(delta22)), 0.260 (Gln H(varepsilon21)) and 0.395 (Gln H(varepsilon22)) ppm GPa(-1) can be observed. In both cases, the pressure dependent shift is larger for the pro-E proton than for the pro-Z proton. Within the limits of error the equilibrium constant for the trans- and cis-conformers at the proline peptide bond is independent of pressure in the pressure range studied.

[Indexed for MEDLINE]

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