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Journal Article

Identification of hydroxyl protons, determination of their exchange dynamics, and characterization of hydrogen bonding in a microcrystallin protein.

MPS-Authors
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Linser,  R.
Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society;

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Fulltext (public)

2000308.pdf
(Publisher version), 3MB

Supplementary Material (public)

2000308_Suppl.pdf
(Supplementary material), 352KB

Citation

Agarwal, V., Linser, R., Fink, U., Faelber, K., & Reif, B. (2010). Identification of hydroxyl protons, determination of their exchange dynamics, and characterization of hydrogen bonding in a microcrystallin protein. Journal of the American Chemical Society, 132(9), 3187-3195. doi:10.1021/ja910167q.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0018-EAF6-0
Abstract
Heteronuclear correlation experiments employing perdeuterated proteins enable the observation of all hydroxyl protons in a microcrystalline protein by MAS solid-state NMR. Dipolar-based sequences allow magnetization transfers that are >50 times faster compared to scalar-coupling-based sequences, which significantly facilitates their assignment. Hydroxyl exchange rates were measured using EXSY-type experiments. We find a biexponential decay behavior for those hydroxyl groups that are involved in side chain−side chain C−O−H···O═C hydrogen bonds. The quantification of the distances between the hydroxyl proton and the carbon atoms in the hydrogen-bonding donor as well as acceptor group is achieved via a REDOR experiment. In combination with X-ray data and isotropic proton chemical shifts, availability of 1H,13C distance information can aid in the quantitative description of the geometry of these hydrogen bonds. Similarly, correlations between backbone amide proton and carbonyl atoms are observed, which will be useful in the analysis of the registry of β-strand arrangement in amyloid fibrils.