[ASAP] Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by 19F NMR and Cryo-EM
Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by 19F NMR and Cryo-EM
Yun Huang, Krishna D. Reddy, Clay Bracken, Biao Qiu, Wenhu Zhan, David Eliezer, and Olga Boudker
https://pubs.acs.org/cms/10.1021/jacs.3c01003/asset/images/medium/ja3c01003_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.3c01003
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[NMR paper] Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by 19F NMR and Cryo-EM
Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by 19F NMR and Cryo-EM
Limited chemical shift dispersion represents a significant barrier to studying multistate equilibria of large membrane proteins by ^(19)F NMR. We describe a novel monofluoroethyl ^(19)F probe that dramatically increases the chemical shift dispersion. The improved conformational sensitivity and line shape enable the detection of previously unresolved states in one-dimensional (1D) ^(19)F NMR spectra of a 134 kDa membrane transporter. Changes in the populations of these states in...
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[NMR paper] Ca(2+) ATPase conformational transitions in lipid bilayers mapped by site-directed ethylation and solid-state NMR.
Ca(2+) ATPase conformational transitions in lipid bilayers mapped by site-directed ethylation and solid-state NMR.
Ca(2+) ATPase conformational transitions in lipid bilayers mapped by site-directed ethylation and solid-state NMR.
ACS Chem Biol. 2015 Dec 9;
Authors: Vostrikov VV, Gustavsson M, Gopinath T, Mullen D, Dicke AA, Truong V, Veglia G
Abstract
To transmit signals across cellular compartments, many membrane-embedded enzymes undergo extensive conformational rearrangements. Monitoring these events in lipid bilayers by...
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Photochemical Pump and NMR Probe: Chemically Created NMR Coherence on a Microsecond Time Scale
Photochemical Pump and NMR Probe: Chemically Created NMR Coherence on a Microsecond Time Scale
Olga Torres, Barbara Procacci, Meghan E. Halse, Ralph W. Adams, Damir Blazina, Simon B. Duckett, Beatriz Eguillor, Richard A. Green, Robin N. Perutz and David C. Williamson
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja504732u/aop/images/medium/ja-2014-04732u_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja504732u
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA ...
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Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supramolecular Protein Systems: Applications to the Proteasome and to the ClpP Protease
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supramolecular Protein Systems: Applications to the Proteasome and to the ClpP Protease
Tomasz L. Religa, Amy M. Ruschak, Rina Rosenzweig and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja202259a/aop/images/medium/ja-2011-02259a_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja202259a
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/rQfCMlQFoW8
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Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
J Am Chem Soc. 2011 May 11;
Authors: Religa TL, Ruschak AM, Rosenzweig R, Kay LE
Methyl groups are powerful reporters of structure, motion and function in NMR studies of supra-molecular protein assemblies. Their...
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[NMR paper] Site-directed 13C solid-state NMR studies on membrane proteins: strategy and goals to
Site-directed 13C solid-state NMR studies on membrane proteins: strategy and goals toward revealing conformation and dynamics as illustrated for bacteriorhodopsin labeled with amino acid residues.
Related Articles Site-directed 13C solid-state NMR studies on membrane proteins: strategy and goals toward revealing conformation and dynamics as illustrated for bacteriorhodopsin labeled with amino acid residues.
Magn Reson Chem. 2004 Feb;42(2):218-30
Authors: Saitô H, Mikami J, Yamaguchi S, Tanio M, Kira A, Arakawa T, Yamamoto K, Tuzi S
We have so...
Posttranslational, site-directed photochemical fluorine editing of protein sidechains to probe residue oxidation state via - Nature.com
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