[NMR paper] Signaling states of a short blue light photoreceptor protein PpSB1-LOV revealed from crystal structures and solution NMR spectroscopy.
Signaling states of a short blue light photoreceptor protein PpSB1-LOV revealed from crystal structures and solution NMR spectroscopy.
Related Articles Signaling states of a short blue light photoreceptor protein PpSB1-LOV revealed from crystal structures and solution NMR spectroscopy.
J Mol Biol. 2016 Jun 9;
Authors: Röllen K, Granzin J, Panwalkar V, Arinkin V, Rani R, Hartmann R, Krauss U, Jaeger KE, Willbold D, Batra-Safferling R
Abstract
LOV (Light-Oxygen-Voltage) domains represent the photo-responsive domains of various...
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06-14-2016 08:23 PM
Signaling states of a short blue light photoreceptor protein PpSB1-LOV revealed from crystal structures and solution NMR spectroscopy
Signaling states of a short blue light photoreceptor protein PpSB1-LOV revealed from crystal structures and solution NMR spectroscopy
Publication date: Available online 9 June 2016
Source:Journal of Molecular Biology</br>
Author(s): Katrin Röllen, Joachim Granzin, Vineet Panwalkar, Vladimir Arinkin, Raj Rani, Rudolf Hartmann, Ulrich Krauss, Karl-Erich Jaeger, Dieter Willbold, Renu Batra-Safferling</br>
LOV (Light-Oxygen-Voltage) domains represent the photo-responsive domains of various blue-light photoreceptor proteins and are widely distributed...
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06-09-2016 06:54 AM
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy [Biophysics and Computational Biology]
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy
Masterson, L. R., Shi, L., Metcalfe, E., Gao, J., Taylor, S. S., Veglia, G....
Date: 2011-04-26
Protein kinase A (PKA) is a ubiquitous phosphoryl transferase that mediates hundreds of cell signaling events. During turnover, its catalytic subunit (PKA-C) interconverts between three major conformational states (open, intermediate, and closed) that are dynamically and allosterically activated by nucleotide binding. We show that the structural transitions between these...
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04-27-2011 04:16 AM
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.
Proc Natl Acad Sci U S A. 2011 Apr 6;
Authors: Masterson LR, Shi L, Metcalfe E, Gao J, Taylor SS, Veglia G
Protein kinase A (PKA) is a ubiquitous phosphoryl transferase that mediates hundreds of cell signaling events. During turnover, its catalytic subunit (PKA-C) interconverts between three major conformational states...