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  Access to aliphatic protons as reporters in non-deuterated proteins by solid-state NMR.

Vasa, S. K., Rovo, P., Giller, K., Becker, S., & Linser, R. (2016). Access to aliphatic protons as reporters in non-deuterated proteins by solid-state NMR. Physical Chemistry Chemical Physics, 18(12), 8359-8363. doi: 10.1039/c5cp06601h.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-42C6-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-268E-C
Genre: Journal Article

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 Creators:
Vasa, S. K.1, Author              
Rovo, P.1, Author              
Giller, K.2, Author              
Becker, S.2, Author              
Linser, R.1, Author              
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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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 Abstract: Interactions within proteins, with their surrounding, and with other molecules are mediated mostly by hydrogen atoms. In fully protonated, inhomogeneous, or larger proteins, however, aliphatic proton shifts tend to show little dispersion despite fast Magic-Angle Spinning. 3D correlations dispersing aliphatic proton shifts by their better resolved amide N/H shifts can alleviate this problem. Using inverse second-order cross-polarization (iSOCP), we here introduce dedicated and improved means to sensitively link site-specific chemical shift information from aliphatic protons with a backbone amide resolution. Thus, even in cases where protein deuteration is impossible, this approach may enable access to various aspects of protein functions that are reported on by protons.

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Language(s): eng - English
 Dates: 2015-11-202016-03-28
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1039/c5cp06601h
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Title: Physical Chemistry Chemical Physics
Source Genre: Journal
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Pages: - Volume / Issue: 18 (12) Sequence Number: - Start / End Page: 8359 - 8363 Identifier: -