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Article Dans Une Revue Journal of Physical Chemistry B Année : 2018

Simple and Robust Study of Backbone Dynamics of Crystalline Proteins Employing H-1-N-15 Dipolar Coupling Dispersion

Résumé

We report a new solid-state multidimensional NMR approach based on the cross-polarization with variable-contact pulse sequence [Paluch, P.; Pawlak, T.; Amoureux, J.-P.; Potrzebowski, M. J. J. Magn. Reson. 233, 2013, 56], with 1H inverse detection and very fast magic angle spinning (νR = 60 kHz), dedicated to the measurement of local molecular motions of 1H–15N vectors. The introduced three-dimensional experiments, 1H–15N–1H and hCA(N)H, are particularly useful for the study of molecular dynamics of proteins and other complex structures. The applicability and power of this methodology have been revealed by employing as a model sample the GB-1 small protein doped with Na2CuEDTA. The results clearly prove that the dispersion of 1H–15N dipolar coupling constants well correlates with higher order structure of the protein. Our approach complements the conventional studies and offers a fast and reasonably simple method.
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Dates et versions

hal-04313245 , version 1 (29-11-2023)

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Piotr Paluch, Tomasz Pawlak, Karol Lawniczak, Julien Trebosc, Olivier Lafon, et al.. Simple and Robust Study of Backbone Dynamics of Crystalline Proteins Employing H-1-N-15 Dipolar Coupling Dispersion. Journal of Physical Chemistry B, 2018, Journal of Physical Chemistry B, 122, pp.8146-8156. ⟨10.1021/acs.jpcb.8b04557⟩. ⟨hal-04313245⟩
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