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Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH2

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Abstract

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 1Hα, 13Cα 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 B 1 and B 2 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.

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Acknowledgments

This work has been supported by the DFG (FOR1979 and KA 647), the Humboldt Society, Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP 2010/01362-5 and 2010/12953-4), and the Human Frontier Science Program Organization (HFSPO).

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Authors and Affiliations

  1. Institute of Biophysics and Physical Biochemistry and Centre of Magnetic Resonance in Chemistry and Biomedicine, University of Regensburg, 93040, Regensburg, Germany

    Markus Beck Erlach, Joerg Koehler, Werner Kremer & Hans Robert Kalbitzer

  2. Physics Institute of São Carlos, University of São Paulo, São Carlos, 13566-590, Brazil

    Edson Crusca Jr. & Claudia E. Munte

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  1. Markus Beck Erlach
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  2. Joerg Koehler
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  4. Werner Kremer
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  6. Hans Robert Kalbitzer
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Correspondence to Hans Robert Kalbitzer.

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Erlach, M.B., Koehler, J., Crusca, E. et al. Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH2 . J Biomol NMR 65, 65–77 (2016). https://doi.org/10.1007/s10858-016-0030-4

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