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  Asynchronous through-bond homonuclear isotropic mixing: Application to carbon-carbon transfer in perdeuterated proteins under MAS.

Kulminskaya, N., Vasa, S. K., Giller, K., Becker, S., & Linser, R. (2015). Asynchronous through-bond homonuclear isotropic mixing: Application to carbon-carbon transfer in perdeuterated proteins under MAS. Journal of Biomolecular NMR, 63(3), 245-253. doi:10.1007/s10858-015-9980-1.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-4CD4-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-58FA-6
Genre: Journal Article

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 Creators:
Kulminskaya, N., Author
Vasa, S. K.1, Author              
Giller, K.2, Author              
Becker, S.2, Author              
Linser, R.1, Author              
Affiliations:
1Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society, ou_1950286              
2Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: SH3 domain; Solid-state NMR (ssNMR); MAS; Homonuclear isotropic mixing; Perdeuterated proteins; MOCCA
 Abstract: Multiple-bond carbon–carbon homonuclear mixing is a hurdle in extensively deuterated proteins and under fast MAS due to the absence of an effective proton dipolar-coupling network. Such conditions are now commonly employed in solid-state NMR spectroscopy. Here, we introduce an isotropic homonuclear 13C–13C through-bond mixing sequence, MOCCA, for the solid state. Even though applied under MAS, this scheme performs without rotor synchronization and thus does not pose the usual hurdles in terms of power dissipation for fast spinning. We compare its performance with existing homonuclear 13C–13C mixing schemes using a perdeuterated and partially proton-backexchanged protein. Based on the analysis of side chain carbon–carbon correlations, we show that particularly MOCCA with standard 180-degree pulses and delays leading to non-rotor-synchronized spacing performs exceptionally well. This method provides high magnetization transfer efficiency for multiple-bond transfer in the aliphatic region compared with other tested mixing sequences. In addition, we show that this sequence can also be tailor-made for recoupling within a selected spectral region using band-selective pulses.

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Language(s): eng - English
 Dates: 2015-08-302015-11
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1007/s10858-015-9980-1
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Project name : A04
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Funding program : SFB803
Funding organization : Deutsche Forschungsgemeinschaft

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Title: Journal of Biomolecular NMR
Source Genre: Journal
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Pages: - Volume / Issue: 63 (3) Sequence Number: - Start / End Page: 245 - 253 Identifier: -