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  Selective 1H-1H distance restraints in fully protonated proteins by very fast magic-angle spinning solid-state NMR.

Jain, M. G., Lalli, D., Stanek, J., Gowda, C., Prakash, S., Schwarzer, T. S., et al. (2017). Selective 1H-1H distance restraints in fully protonated proteins by very fast magic-angle spinning solid-state NMR. Journal of Physical Chemistry Letters, 8(11), 2399-2405. doi:10.1021/acs.jpclett.7b00983.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-60F2-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-6112-8
Genre: Journal Article

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 Creators:
Jain, M. G., Author
Lalli, D., Author
Stanek, J., Author
Gowda, C., Author
Prakash, S., Author
Schwarzer, T. S., Author
Schubeis, T., Author
Castiglione, K., Author
Andreas, L.1, Author              
Madhu, P. K., Author
Pintacuda, G., Author
Agarwal, V., Author
Affiliations:
1Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society, ou_2396693              

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 Abstract: Very fast magic-angle spinning (MAS > 80 kHz) NMR combined with high-field magnets has enabled the acquisition of proton-detected spectra in fully protonated solid samples with sufficient resolution and sensitivity. One of the primary challenges in structure determination of protein is observing long-range 1H-1H contacts. Here we use band-selective spin-lock pulses to obtain selective 1H-1H contacts (e.g., HN-HN) on the order of 5-6 Å in fully protonated proteins at 111 kHz MAS. This approach is a major advancement in structural characterization of proteins given that magnetization can be selectively transferred between protons that are 5-6 Å apart despite the presence of other protons at shorter distance. The observed contacts are similar to those previously observed only in perdeuterated proteins with selective protonation. Simulations and experiments show the proposed method has performance that is superior to that of the currently used methods. The method is demonstrated on GB1 and a β-barrel membrane protein, AlkL.

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Language(s): eng - English
 Dates: 2017-05-112017-06-01
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/acs.jpclett.7b00983
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Title: Journal of Physical Chemistry Letters
Source Genre: Journal
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Pages: - Volume / Issue: 8 (11) Sequence Number: - Start / End Page: 2399 - 2405 Identifier: -