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  Backbone assignment for minimal protein amounts of low structural homogeneity in the absence of deuteration.

Xiang, S., Biernat, J., Mandelkow, E., Becker, S., & Linser, R. (2016). Backbone assignment for minimal protein amounts of low structural homogeneity in the absence of deuteration. Chemical Communications, 52(21), 4002-4005. doi:10.1039/C5CC09160H.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0029-60E0-7 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002D-296D-B
Genre: Journal Article

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 Creators:
Xiang, S.1, Author           
Biernat, J., Author
Mandelkow, E., 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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 Abstract: NMR characterization of many proteins is limited by low expression, hurdles for deuteration, and poor sample homogeneity. We introduce a set of high-dimensionality proton-detected experiments developed for unambiguous resonance assignments of such proteins, which we could successfully apply to a 1-mg amount of non-deuterated Tau paired helical filaments.

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Language(s): eng - English
 Dates: 2016-01-192016-03-14
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1039/C5CC09160H
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Title: Chemical Communications
Source Genre: Journal
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Pages: - Volume / Issue: 52 (21) Sequence Number: - Start / End Page: 4002 - 4005 Identifier: -