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  Proton transverse relaxation as a sensitive probe for structure determination in solid proteins.

Rovo, P., Grohe, K., Giller, K., Becker, S., & Linser, R. (2015). Proton transverse relaxation as a sensitive probe for structure determination in solid proteins. ChemPhysChem, 16(18), 3791-3796. doi:10.1002/cphc.201500799.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-5B1F-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-7A4D-7
Genre: Journal Article

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 Creators:
Rovo, P.1, Author              
Grohe, 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: paramagnetic relaxation enhancement, MTSL spin label, solid-state NMR spectroscopy, protein structure determination
 Abstract: Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy has been used successfully to elucidate atomic-resolution structures of insoluble proteins. However, the major bottleneck is the difficulty to obtain valuable long-distance structural information. Here we propose to use distance restraints as long as 32 Å obtained from quantification of transverse proton relaxation induced by a methanethiosulfonate spin label (MTSL). Combined with dipolar proton-proton distance restraints, we are able to obtain a protein structure with excellent precision from a single spin-labeled protein sample of an amount of 1 mg under fast magic angle spinning.

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Language(s): eng - English
 Dates: 2015-10-012015-12-21
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/cphc.201500799
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Title: ChemPhysChem
Source Genre: Journal
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Pages: - Volume / Issue: 16 (18) Sequence Number: - Start / End Page: 3791 - 3796 Identifier: -