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Default Characterization of the ground state dynamics of proteorhodopsin by NMR and optical spectroscopies

Characterization of the ground state dynamics of proteorhodopsin by NMR and optical spectroscopies


Abstract We characterized the dynamics of proteorhodopsin (PR), solubilized in diC7PC, a detergent micelle, by liquid-state NMR spectroscopy at T = 323 K. Insights into the dynamics of PR at different time scales could be obtained and dynamic hot spots could be identified at distinct, functionally relevant regions of the protein, including the BC loop, the EF loop, the N-terminal part of helix F and the C-terminal part of helix G. We further characterize the dependence of the photocycle on different detergents (n-Dodecyl β-D-maltoside DDM; 1,2-diheptanoyl-sn-glycero-3-phosphocholine diC7PC) by ultrafast time-resolved UV/VIS spectroscopy. While the photocycle intermediates of PR in diC7PC and DDM exhibit highly similar spectral characteristics, significant changes in the population of these intermediates are observed. In-situ NMR experiments have been applied to characterize structural changes during the photocycle. Light-induced chemical shift changes detected during the photocycle in diC7PC are very small, in line with the changes in the population of intermediates in the photocycle of proteorhodopsin in diC7PC, where the late O-intermediate populated in DDM is missing and the population is shifted towards an equilibrium of intermediates states (M, N, O) without accumulation of a single populated intermediate.

  • Content Type Journal Article
  • Category Article
  • Pages 1-13
  • DOI 10.1007/s10858-012-9684-8
  • Authors
    • Jochen Stehle, Institute for Organic Chemistry and Chemical Biology, Goethe University Frankfurt, 60438 Frankfurt, Germany
    • Frank Scholz, Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt, 60438 Frankfurt, Germany
    • Frank Löhr, Institute of Biophysical Chemistry, Goethe University Frankfurt, 60438 Frankfurt, Germany
    • Sina Reckel, Institute of Biophysical Chemistry, Goethe University Frankfurt, 60438 Frankfurt, Germany
    • Christian Roos, Institute of Biophysical Chemistry, Goethe University Frankfurt, 60438 Frankfurt, Germany
    • Michaela Blum, Institute of Biophysical Chemistry, Goethe University Frankfurt, 60438 Frankfurt, Germany
    • Markus Braun, Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt, 60438 Frankfurt, Germany
    • Clemens Glaubitz, Institute of Biophysical Chemistry, Goethe University Frankfurt, 60438 Frankfurt, Germany
    • Volker Dötsch, Institute of Biophysical Chemistry, Goethe University Frankfurt, 60438 Frankfurt, Germany
    • Josef Wachtveitl, Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt, 60438 Frankfurt, Germany
    • Harald Schwalbe, Institute for Organic Chemistry and Chemical Biology, Goethe University Frankfurt, 60438 Frankfurt, Germany


Source: Journal of Biomolecular NMR
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