Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets-Reference-Cited by-同舟云学术

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Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets

Published:2013-08-14 Issue:1 Volume:57 Page:65-72
ISSN:0925-2738
Container-title:Journal of Biomolecular NMR
language:en
Short-container-title:J Biomol NMR

Author:

Bellstedt Peter,Seiboth Thomas,Häfner Sabine,Kutscha Henriette,Ramachandran Ramadurai,Görlach Matthias

Publisher

Springer Science and Business Media LLC

Subject

Spectroscopy,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s10858-013-9768-0.pdf

Reference40 articles.

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2. Banigan JR, Gayen A, Traaseth NJ (2013) Combination of 15N reverse labeling and afterglow spectroscopy for assigning membrane protein spectra by magic-angle-spinning solid-state NMR: application to the multidrug resistance protein EmrE. J Biomol NMR 55(4):391–399

3. Bracken C, Palmer AG, Cavanagh J (1997) (H)N(COCA)NH and HN(COCA)NH experiments for 1H-15N backbone assignments in 13C/15N-labeled proteins. J Biomol NMR 9(1):94–100

4. Coggins BE, Venters RA, Zhou P (2010) Radial sampling for fast NMR: concepts and practices over three decades. Prog Nucl Magn Reson Spectrosc 57(4):381–419

5. Date H, Onodera O, Tanaka H, Iwabuchi K, Uekawa K, Igarashi S, Koike R, Hiroi T, Yuasa T, Awaya Y, Sakai T, Takahashi T, Nagatomo H, Sekijima Y, Kawachi I, Takiyama Y, Nishizawa M, Fukuhara N, Saito K, Sugano S, Tsuji S (2001) Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is caused by mutations in a new HIT superfamily gene. Nat Genet 29(2):184–188

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