Sparse pseudocontact shift NMR data obtained from a non-canonical amino acid-linked lanthanide tag improves integral membrane protein structure prediction-Reference-Cited by-同舟云学术

Sparse pseudocontact shift NMR data obtained from a non-canonical amino acid-linked lanthanide tag improves integral membrane protein structure prediction

Published:2023-04-04 Issue:3 Volume:77 Page:69-82
ISSN:0925-2738
Container-title:Journal of Biomolecular NMR
language:en
Short-container-title:J Biomol NMR

Author:

Ledwitch Kaitlyn V.,Künze Georg,McKinney Jacob R.,Okwei Elleansar,Larochelle Katherine,Pankewitz Lisa,Ganguly Soumya,Darling Heather L.,Coin Irene,Meiler Jens

Funder

National Institutes of Health

Deutsche Forschungsgemeinschaft

Publisher

Springer Science and Business Media LLC

Subject

Spectroscopy,Biochemistry

Link

https://link.springer.com/content/pdf/10.1007/s10858-023-00412-9.pdf

Reference57 articles.

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3. Crick DJ et al (2015) Integral membrane protein structure determination using pseudocontact shifts. J Biomol NMR 61:197–207

4. de la Cruz L et al (2011) Binding of low molecular weight inhibitors promotes large conformational changes in the dengue virus NS2B-NS3 protease: fold analysis by pseudocontact shifts. J Am Chem Soc 133:19205–19215

5. Fernandez C, Hilty C, Wider G, Guntert P, Wuthrich K (2004) NMR structure of the integral membrane protein OmpX. J Mol Biol 336:1211–1221

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