Pressure dependence of backbone chemical shifts in the model peptides Ac Gly Gly Xxx Ala NH2
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 1Ha, 13Ca and 13C' 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 B1 and B2 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.Graphical Abstract
Journal of biomolecular NMR