Detection of Metabolite–Protein Interactions in Complex Biological Samples by High-Resolution Relaxometry: Toward Interactomics by NMR - ACS Publications
Detection of Metabolite–Protein Interactions in Complex Biological Samples by High-Resolution Relaxometry: Toward Interactomics by NMR - ACS Publications
Detection of Metabolite–Protein Interactions in Complex Biological Samples by High-Resolution Relaxometry: Toward Interactomics by NMR - ACS Publications
How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?
How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?
Abstract
The dynamics of molecules in solution is usually quantified by the determination of timescale-specific amplitudes of motions. High-resolution nuclear magnetic resonance (NMR) relaxometry experimentsâ??where the sample is transferred to low fields for longitudinal (T1) relaxation, and back to high field for detection with residue-specific resolutionâ??seeks to increase the ability to distinguish the contributions from motion on...
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03-23-2021 07:56 PM
[NMR paper] Dynamic characteristics of GMP reductase complexes revealed by high resolution 31P field cycling NMR relaxometry.
Dynamic characteristics of GMP reductase complexes revealed by high resolution 31P field cycling NMR relaxometry.
Dynamic characteristics of GMP reductase complexes revealed by high resolution 31P field cycling NMR relaxometry.
Biochemistry. 2018 Mar 16;:
Authors: Rosenberg MM, Redfield AG, Roberts M, Hedstrom L
Abstract
The ability of enzymes to modulate the dynamics of bound substrates and cofactors is a critical feature of catalysis, but the role of dynamics has largely been approached from the perspective of the protein....
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03-17-2018 12:12 PM
High sensitivity high-resolution full range relaxometry using a fast mechanical sample shuttling device and a cryo-probe
High sensitivity high-resolution full range relaxometry using a fast mechanical sample shuttling device and a cryo-probe
Abstract
Field-dependent NMR studies of bio-molecular systems using a sample shuttling hardware operating on a high-field NMR apparatus have provided valuable structural and dynamic information. We have recently published a design of a compact sample transportation device, called â??field-cyclerâ??, which was installed in a commercial spectrometer and which provided highly precise positioning and stability during high speed...
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11-19-2016 08:35 PM
Systematic Identification of Protein–Metabolite Interactions in Complex MetaboliteMixtures by Ligand-Detected Nuclear Magnetic Resonance Spectroscopy
Systematic Identification of Protein–Metabolite Interactions in Complex MetaboliteMixtures by Ligand-Detected Nuclear Magnetic Resonance Spectroscopy
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01291/20160425/images/medium/bi-2015-012916_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01291
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04-26-2016 12:14 PM
[NMR paper] Systematic identification of protein-metabolite interactions in complex metabolite mixtures by ligand-detected NMR spectroscopy.
Systematic identification of protein-metabolite interactions in complex metabolite mixtures by ligand-detected NMR spectroscopy.
Systematic identification of protein-metabolite interactions in complex metabolite mixtures by ligand-detected NMR spectroscopy.
Biochemistry. 2016 Apr 11;
Authors: Nikolaev YV, Kochanowski K, Link H, Sauer U, Allain FH
Abstract
Protein-metabolite interactions play a vital role in the regulation of numerous cellular processes. Consequently, identifying such interactions is a key prerequisite for...
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04-12-2016 09:12 PM
NanosecondTime Scale Motions in Proteins Revealedby High-Resolution NMR Relaxometry
NanosecondTime Scale Motions in Proteins Revealedby High-Resolution NMR Relaxometry
Cyril Charlier, Shahid Nawaz Khan, Thorsten Marquardsen, Philippe Pelupessy, Volker Reiss, Dimitris Sakellariou, Geoffrey Bodenhausen, Frank Engelke and Fabien Ferrage
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja409820g/aop/images/medium/ja-2013-09820g_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja409820g
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http://feeds.feedburner.com/~r/acs/jacsat/~4/QcFGZznyEp0
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11-27-2013 01:50 AM
[NMR paper] Nanosecond timescale motions in proteins revealed by high-resolution NMR relaxometry.
Nanosecond timescale motions in proteins revealed by high-resolution NMR relaxometry.
Related Articles Nanosecond timescale motions in proteins revealed by high-resolution NMR relaxometry.
J Am Chem Soc. 2013 Nov 14;
Authors: Charlier CD, Khan SN, Marquardsen T, Pelupessy P, Reiss V, Sakellariou D, Bodenhausen G, Engelke F, Ferrage F
Abstract
Understanding the molecular determinants underlying protein function requires the characterization of both structure and dynamics at atomic resolution. Nuclear relaxation rates allow a precise...
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11-16-2013 03:14 PM
Simultaneous Detection of Protein Phosphorylation and Acetylation by High-Resolution
Simultaneous Detection of Protein Phosphorylation and Acetylation by High-Resolution NMR Spectroscopy
Stamatios Liokatis, Alexander Dose, Dirk Schwarzer and Philipp Selenko
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja106764y/aop/images/medium/ja-2010-06764y_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja106764y
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/jfhp2Sg-hpY