Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy-Reference-Cited by-同舟云学术

Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy

Published:2013-08-21 Issue:2 Volume:57 Page:91-102
ISSN:0925-2738
Container-title:Journal of Biomolecular NMR
language:en
Short-container-title:J Biomol NMR

Author:

Mote Kaustubh R.,Gopinath T.,Veglia Gianluigi

Publisher

Springer Science and Business Media LLC

Subject

Spectroscopy,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s10858-013-9766-2.pdf

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3. Buck B, Zamoon J, Kirby TL, DeSilva TM, Karim C, Thomas D, Veglia G (2003) Overexpression, purification, and characterization of recombinant Ca-ATPase regulators for high-resolution solution and solid-state NMR studies. Protein Expr Purif 30:253–261

4. Buffy JJ, Buck-Koehntop BA, Porcelli F, Traaseth NJ, Thomas DD, Veglia G (2006a) Defining the intramembrane binding mechanism of sarcolipin to calcium ATPase using solution NMR spectroscopy. J Mol Biol 358:420–429

5. Buffy JJ, Traaseth NJ, Mascioni A, Gor’kov PL, Chekmenev EY, Brey WW, Veglia G (2006b) Two-dimensional solid-state NMR reveals two topologies of sarcolipin in oriented lipid bilayers. Biochemistry 45:10939–10946

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