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  Protein conformational dynamics studied by 15N and 1H R relaxation dispersion: Application to wild-type and G53A ubiquitin crystals.

Gauto, D. F., Hessel, A., Kurauskas, V., Linser, R., & Schanda, P. (2017). Protein conformational dynamics studied by 15N and 1H R relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance, 87, 86-95. doi:10.1016/j.ssnmr.2017.04.002.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-312A-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-372F-4
Genre: Journal Article

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 Creators:
Gauto, D. F., Author
Hessel, A., Author
Kurauskas, V., Author
Linser, R.1, Author              
Schanda, P., Author
Affiliations:
1Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society, ou_1950286              

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 Abstract: Solid-state NMR spectroscopy can provide site-resolved information about protein dynamics over many time scales. Here we combine protein deuteration, fast magic-angle spinning (~45–60 kHz) and proton detection to study dynamics of ubiquitin in microcrystals, and in particular a mutant in a region that undergoes microsecond motions in a β-turn region in the wild-type protein. We use 15N R1ρ relaxation measurements as a function of the radio-frequency (RF) field strength, i.e. relaxation dispersion, to probe how the G53A mutation alters these dynamics. We report a population-inversion of conformational states: the conformation that in the wild-type protein is populated only sparsely becomes the predominant state. We furthermore explore the potential to use amide-1H R1ρ relaxation to obtain insight into dynamics. We show that while quantitative interpretation of 1H relaxation remains beyond reach under the experimental conditions, due to coherent contributions to decay, one may extract qualitative information about flexibility.

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Language(s): eng - English
 Dates: 2017-04-142017-10
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.ssnmr.2017.04.002
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Title: Solid State Nuclear Magnetic Resonance
Source Genre: Journal
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Pages: - Volume / Issue: 87 Sequence Number: - Start / End Page: 86 - 95 Identifier: -