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Journal Article

Fractional deuteration applied to biomolecular solid-state NMR spectroscopy.


Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

(Publisher version), 1021KB

Supplementary Material (public)

(Supplementary material), 351KB


Nand, D., Cukkemane, A., Becker, S., & Baldus, M. (2012). Fractional deuteration applied to biomolecular solid-state NMR spectroscopy. Journal of Biomolecular NMR, 52(2), 91-101. doi:10.1007/s10858-011-9585-2.

Cite as: http://hdl.handle.net/11858/00-001M-0000-000F-843A-6
Solid-state Nuclear Magnetic Resonance can provide detailed insight into structural and dynamical aspects of complex biomolecules. With increasing molec- ular size, advanced approaches for spectral simplification and the detection of medium to long-range contacts become of critical relevance. We have analyzed the pro- tonation pattern of a membrane-embedded ion channel that was obtained from bacterial expression using protonated precursors and D 2 O medium. We find an overall reduction of 50% in protein protonation. High levels of deuteration at H a and H b positions reduce spectral congestion in ( 1 H, 13 C, 15 N) correlation experiments and generate a transfer profile in longitudinal mixing schemes that can be tuned to specific resonance frequencies. At the same time, residual protons are predominantly found at amino-acid side-chain positions enhancing the prospects for obtaining side-chain resonance assignments and for detecting med- ium to long-range contacts. Fractional deuteration thus provides a powerful means to aid the structural analysis of complex biomolecules by solid-state NMR.