[NMR paper] Measurement of State-Specific Association Constants in Allosteric Sensors through Molecular Stapling and NMR.
Measurement of State-Specific Association Constants in Allosteric Sensors through Molecular Stapling and NMR.
Related Articles Measurement of State-Specific Association Constants in Allosteric Sensors through Molecular Stapling and NMR.
J Am Chem Soc. 2015 Aug 6;
Authors: Moleschi KJ, Akimoto M, Melacini G
Abstract
Allostery is a ubiquitous mechanism to control biological function and arises from the coupling of inhibitory and binding equilibria. The extent of coupling reflects the inactive vs. active state selectivity of the...
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08-08-2015 12:17 PM
[NMR paper] Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins.
Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins.
Related Articles Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins.
Curr Opin Struct Biol. 2015 Apr 13;32:113-122
Authors: Kerfah R, Plevin MJ, Sounier R, Gans P, Boisbouvier J
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is a uniquely powerful tool for studying the structure, dynamics and interactions of biomolecules at atomic resolution. In the past 15 years, the...
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04-17-2015 08:49 PM
Hyperpolarized Xenon-Based Molecular Sensors for Label-Free Detection of analytes
From The DNP-NMR Blog:
Hyperpolarized Xenon-Based Molecular Sensors for Label-Free Detection of analytes
Garimella, P.D., et al., Hyperpolarized Xenon-Based Molecular Sensors for Label-Free Detection of analytes. J. Am. Chem. Soc., 2013. 136(1): p. 164-168.
http://pubs.acs.org/doi/abs/10.1021/ja406760r
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Highly Precise Measurementof Kinetic Isotope EffectsUsing 1H-Detected 2D [13C,1H]-HSQC NMR Spectroscopy
Highly Precise Measurementof Kinetic Isotope EffectsUsing 1H-Detected 2D -HSQC NMR Spectroscopy
Kathryn A. Manning, Bharathwaj Sathyamoorthy, Alexander Eletsky, Thomas Szyperski and Andrew S. Murkin
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja310353c/aop/images/medium/ja-2012-10353c_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja310353c
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/kfh2aVSYThA
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12-12-2012 08:19 AM
Site-Resolved Measurementof Microsecond-to-MillisecondConformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy
Site-Resolved Measurementof Microsecond-to-MillisecondConformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy
Martin Tollinger, Astrid C. Sivertsen, Beat H. Meier, Matthias Ernst and Paul Schanda
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja303591y/aop/images/medium/ja-2012-03591y_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja303591y
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ZVmFwVkbuRs
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[NMR paper] Residue-specific real-time NMR diffusion experiments define the association states of
Residue-specific real-time NMR diffusion experiments define the association states of proteins during folding.
Related Articles Residue-specific real-time NMR diffusion experiments define the association states of proteins during folding.
J Am Chem Soc. 2002 Jun 19;124(24):7156-62
Authors: Buevich AV, Baum J
Characterizing the association states of proteins during folding is critical for understanding the nature of protein-folding intermediates and protein-folding pathways, protein aggregation, and disease-related aggregation. To study the...
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11-24-2010 08:49 PM
[NMR paper] NMR exchange broadening arising from specific low affinity protein self-association:
NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1.
Related Articles NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1.
J Biomol NMR. 1999 Aug;14(4):307-20
Authors: Pfuhl M, Chen HA, Kristensen SM, Driscoll PC
Nuclear spin relaxation monitored by heteronuclear NMR provides a useful method to probe the overall and internal molecular motion for...
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11-18-2010 08:31 PM
NMR Reveals Two-Step Association of Congo Red to Amyloid ? in Low-Molecular-Weight Ag
NMR Reveals Two-Step Association of Congo Red to Amyloid ? in Low-Molecular-Weight Aggregates.
Related Articles NMR Reveals Two-Step Association of Congo Red to Amyloid ? in Low-Molecular-Weight Aggregates.
J Phys Chem B. 2010 Nov 15;
Authors: Pedersen MO, Mikkelsen K, Behrens MA, Pedersen JS, Enghild JJ, Skrydstrup T, Malmendal A, Nielsen NC
Aggregation of the Amyloid ? peptide into amyloid fibrils is closely related to development of Alzheimer's disease. Many small aromatic compounds have been found to act as inhibitors of fibril formation, and...
Measurementof State-Specific Association Constantsin Allosteric Sensors through Molecular Stapling and NMR
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