Related ArticlesLight-induced uncaging for time-resolved observations of biochemical reactions by MAS NMR spectroscopy.
Chemistry. 2020 Apr 02;:
Authors: de Mos J, Jakob A, Becker-Baldus J, Heckel A, Glaubitz C
Abstract
Light-induced activation of biomolecules by uncaging of photolabile protection groups has found many applications for triggering biochemical reactions with minimal perturbations directly within cells. Such an approach might also offer unique advantages for solid-state NMR experiments on membrane proteins when initiating reactions within or at the membrane directly within the closed MAS rotor. Here, we demonstrate that the integral membrane protein E. coli diacylglycerol kinase (DgkA), which catalyzes the phosphorylation of diacylglycerol, can be controlled by light under MAS-NMR conditions. Uncaging of NPE-ATP or of lipid substrate NPE-DOG by in situ illumination triggers its enzymatic activity, which can be monitored by real-time 31 P-MAS NMR. This proof-of-concept illustrates that combing MAS-NMR with uncaging strategies and illumination methods offers new possibility for controlling biochemical reactions in situ.
PMID: 32240561 [PubMed - as supplied by publisher]
[NMR paper] Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Related Articles Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Angew Chem Int Ed Engl. 2001 Nov 19;40(22):4248-4251
Authors: Wirmer J, Kühn T, Schwalbe H
Abstract
Aspects of the structure of the intermediate populated after 200 ms in the Ca2+ -induced refolding of ?-lactalbumin have been...
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05-03-2018 06:46 PM
Dissolution dynamic nuclear polarization–enhanced magnetic resonance spectroscopy and imaging: Chemical and biochemical reactions in nonequilibrium conditions #DNPNMR
From The DNP-NMR Blog:
Dissolution dynamic nuclear polarization–enhanced magnetic resonance spectroscopy and imaging: Chemical and biochemical reactions in nonequilibrium conditions #DNPNMR
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Lee, Y., Dissolution dynamic nuclear polarization–enhanced magnetic resonance spectroscopy and imaging: Chemical and biochemical reactions in nonequilibrium conditions. Applied Spectroscopy Reviews, 2015. 51(3): p. 210-226.
https://doi.org/10.1080/05704928.2015.1116078
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12-30-2016 04:53 PM
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] Differentially Isotope-Labeled Nucleosomes to Study Asymmetric Histone Modification Crosstalk by Time-Resolved NMR Spectroscopy.
Differentially Isotope-Labeled Nucleosomes to Study Asymmetric Histone Modification Crosstalk by Time-Resolved NMR Spectroscopy.
Related Articles Differentially Isotope-Labeled Nucleosomes to Study Asymmetric Histone Modification Crosstalk by Time-Resolved NMR Spectroscopy.
Angew Chem Int Ed Engl. 2016 May 24;
Authors: Liokatis S, Klingberg R, Tan S, Schwarzer D
Abstract
Post-translational modifications (PTMs) of histones regulate chromatin structure and function. Because nucleosomes contain two copies each of the four core...
[NMR paper] Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.
Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.
Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.
Nat Protoc. 2013 Jun 27;8(7):1416-1432
Authors: Theillet FX, Rose HM, Liokatis S, Binolfi A, Thongwichian R, Stuiver M, Selenko P
Abstract
We outline NMR protocols for site-specific mapping and time-resolved monitoring of...
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06-29-2013 11:49 AM
Site-Specific Mapping and Time-Resolved Monitoring of Lysine Methylation by High-Resolution NMR Spectroscopy
Site-Specific Mapping and Time-Resolved Monitoring of Lysine Methylation by High-Resolution NMR Spectroscopy
Franc?ois-Xavier Theillet, Stamatios Liokatis, Jan Oliver Jost, Beata Bekei, Honor May Rose, Andres Binolfi, Dirk Schwarzer and Philipp Selenko
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja301895f/aop/images/medium/ja-2012-01895f_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja301895f
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http://feeds.feedburner.com/~r/acs/jacsat/~4/tV2dPnMa4Qc