[NMR paper] A general mechanism of photoconversion of green-to-red fluorescent proteins based on blue and infrared light reduces phototoxicity in live-cell single-molecule imaging
A general mechanism of photoconversion of green-to-red fluorescent proteins based on blue and infrared light reduces phototoxicity in live-cell single-molecule imaging
Photoconversion of fluorescent proteins by blue and complementary near-infrared light, termed primed conversion (PC), is a mechanism recently discovered for Dendra2. We demonstrate that controlling the conformation of arginine at residue 66 by threonine at residue 69 of fluorescent proteins from Anthozoan families (Dendra2, mMaple, Eos, mKikGR, pcDronpa protein families) represents a general route to facilitate PC....
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06-02-2017 08:33 PM
[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
Photochemical Reactions of the LOV and LOV-LinkerDomains of the Blue Light Sensor Protein YtvA
Photochemical Reactions of the LOV and LOV-LinkerDomains of the Blue Light Sensor Protein YtvA
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00263/20160527/images/medium/bi-2016-00263j_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00263
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/or4L4jAycnA
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05-28-2016 01:48 PM
[NMR paper] Active-site structure of the thermophilic foc-subunit ring in membranes elucidated by solid-state NMR.
Active-site structure of the thermophilic foc-subunit ring in membranes elucidated by solid-state NMR.
Active-site structure of the thermophilic foc-subunit ring in membranes elucidated by solid-state NMR.
Biophys J. 2014 Jan 21;106(2):390-8
Authors: Kang SJ, Todokoro Y, Yumen I, Shen B, Iwasaki I, Suzuki T, Miyagi A, Yoshida M, Fujiwara T, Akutsu H
Abstract
FoF1-ATP synthase uses the electrochemical potential across membranes or ATP hydrolysis to rotate the Foc-subunit ring. To elucidate the underlying mechanism, we carried out a...
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01-28-2014 11:53 AM
[NMR paper] Solid-state NMR structure determination of whole anchoring threads from the blue mussel Mytilus edulis.
Solid-state NMR structure determination of whole anchoring threads from the blue mussel Mytilus edulis.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Solid-state NMR structure determination of whole anchoring threads from the blue mussel Mytilus edulis.
Biomacromolecules. 2013 Jan 14;14(1):132-41
Authors: Arnold AA, Byette F, Séguin-Heine MO, Leblanc A, Sleno L, Tremblay R, Pellerin C, Marcotte I
Abstract
The molecular structure of the blue mussel Mytilus...
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10-18-2013 06:23 PM
[NMR paper] An NMR comparison of the light-harvesting complex II (LHCII) in active and photoprotective states reveals subtle changes in the chlorophyll a ground-state electronic structures.
An NMR comparison of the light-harvesting complex II (LHCII) in active and photoprotective states reveals subtle changes in the chlorophyll a ground-state electronic structures.
Related Articles An NMR comparison of the light-harvesting complex II (LHCII) in active and photoprotective states reveals subtle changes in the chlorophyll a ground-state electronic structures.
Biochim Biophys Acta. 2013 Mar 4;
Authors: Pandit A, Reus M, Morosinotto T, Bassi R, Holzwarth AR, de Groot HJ
Abstract
To protect the photosynthetic apparatus against...
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03-08-2013 10:35 PM
[NMR paper] The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate s
The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site.
Related Articles The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site.
Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):13025-30
Authors: Kelly MJ, Ball LJ, Krieger C, Yu Y, Fischer M, Schiffmann S, Schmieder P, Kühne R, Bermel W, Bacher A, Richter G, Oschkinat H
Recent developments in...
Dimeric Structure of the Blue Light Sensor ProteinPhotozipper in the Active State
Linear Mode
