1H/13C/15N triple-resonance experiments for structure determinaton of membrane proteins by oriented-sample NMR-Reference-Cited by-同舟云学术

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1H/13C/15N triple-resonance experiments for structure determinaton of membrane proteins by oriented-sample NMR

Published:2021-02 Issue: Volume:111 Page:101701
ISSN:0926-2040
Container-title:Solid State Nuclear Magnetic Resonance
language:en
Short-container-title:Solid State Nuclear Magnetic Resonance

Author:

Lapin Joel,Awosanya Emmanuel O.,Esteves Richard J.A.,Nevzorov Alexander A.

Funder

Army Research Office

Directorate for Biological Sciences

Publisher

Elsevier BV

Subject

Instrumentation,Nuclear and High Energy Physics,General Chemistry,Radiation

Reference58 articles.

1. Fd coat protein structure in membrane environments;McDonnell;J. Mol. Biol.,1993

2. Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy;Opella;Nat. Struct. Biol.,1999

3. Structure of the transmembrane region of the M2 protein H+ channel;Wang;Prot. Sci.,2001

4. Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints;Marassi;Prot. Sci.,2003

5. Structural dynamics and topology of phospholamban in oriented lipid bilayers using multidimensional solid-state NMR;Traaseth;Biochemistry,2006

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