Publication date: Available online 21 January 2014 Source:Journal of Magnetic Resonance
Author(s): D.T. Murray , I. Hung , T.A. Cross
Oriented sample solid state NMR techniques have been routinely employed to determine the structures of membrane proteins with one or two transmembrane helices. For larger proteins the technique has been limited by spectral resolution and lack of assignment strategies. Here, a strategy for resonance assignment is devised and applied to a three transmembrane helix protein. Sequence specific assignments for all labeled transmembrane amino acid sites are obtained, which provide a set of orientational restraints and helix orientation in the bilayer. Our experiments expand the utility of solid state NMR in membrane protein structure characterization to three transmembrane helix proteins and represent a straightforward strategy for routinely characterizing multiple transmembrane helix protein structures. Graphical abstract
[NMR paper] Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.
Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.
Related Articles Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.
J Biomol NMR. 2013 Dec 20;
Authors: Lu GJ, Opella SJ
Abstract
Oriented sample solid-state NMR spectroscopy can be used to determine the three-dimensional structures of membrane proteins in magnetically or mechanically aligned lipid bilayers. The...
nmrlearner
Journal club
0
12-21-2013 03:15 PM
[NMR paper] NMR-based approach to measure the free energy of transmembrane helix-helix interactions.
NMR-based approach to measure the free energy of transmembrane helix-helix interactions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR-based approach to measure the free energy of transmembrane helix-helix interactions.
Biochim Biophys Acta. 2013 Sep 10;
Authors: Mineev KS, Lesovoy DM, Usmanova DR, Goncharuk SA, Shulepko MA, Lyukmanova EN, Kirpichnikov MP, Bocharov EV, Arseniev AS
Abstract
Knowledge of the energetic parameters of transmembrane...
Magic Angle Spinning and Oriented Sample Solid-State NMR Structural Restraints Combine for Influenza A M2 Protein Functional Insights
Magic Angle Spinning and Oriented Sample Solid-State NMR Structural Restraints Combine for Influenza A M2 Protein Functional Insights
Thach V. Can, Mukesh Sharma, Ivan Hung, Peter L. Gor’kov, William W. Brey and Timothy A. Cross
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja3004039/aop/images/medium/ja-2012-004039_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja3004039
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/xappAmN-wb8
[NMR paper] Complete assignment of heteronuclear protein resonances by protonless NMR spectroscop
Complete assignment of heteronuclear protein resonances by protonless NMR spectroscopy.
Related Articles Complete assignment of heteronuclear protein resonances by protonless NMR spectroscopy.
Angew Chem Int Ed Engl. 2005 May 13;44(20):3089-92
Authors: Bermel W, Bertini I, Duma L, Felli IC, Emsley L, Pierattelli R, Vasos PR
Assignment of Oriented Sample NMR Resonances from a Three Transmembrane Helix Protein
Highlights
Linear Mode
