Proton polarization in photo-excited aromatic molecule at room temperature enhanced by intense optical source and temperature control
From The DNP-NMR Blog:
Proton polarization in photo-excited aromatic molecule at room temperature enhanced by intense optical source and temperature control
Sakaguchi, S., et al., Proton polarization in photo-excited aromatic molecule at room temperature enhanced by intense optical source and temperature control. Nuclear Instruments and Methods in Physics Research Section B: Beam Interactions with Materials and Atoms, 2013(0).
http://www.sciencedirect.com/science/article/pii/S0168583X13008872
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11-21-2013 01:14 AM
Computational Study andMolecular Orbital Analysisof NMR Shielding, Spin–Spin Coupling, and Electric Field Gradientsof Azido Platinum Complexes
Computational Study andMolecular Orbital Analysisof NMR Shielding, Spin–Spin Coupling, and Electric Field Gradientsof Azido Platinum Complexes
Kiplangat Sutter and Jochen Autschbach
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja3040762/aop/images/medium/ja-2012-040762_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja3040762
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http://feeds.feedburner.com/~r/acs/jacsat/~4/XTeiJ4ddvO4
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08-04-2012 05:22 AM
Quantitative Analysisof Multisite Protein–LigandInteractions by NMR: Binding of Intrinsically Disordered p53 TransactivationSubdomains with the TAZ2 Domain of CBP
Quantitative Analysisof Multisite Protein–LigandInteractions by NMR: Binding of Intrinsically Disordered p53 TransactivationSubdomains with the TAZ2 Domain of CBP
Munehito Arai, Josephine C. Ferreon and Peter E. Wright
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja209936u/aop/images/medium/ja-2011-09936u_0012.gif
Journal of the American Chemical Society
DOI: 10.1021/ja209936u
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http://feeds.feedburner.com/~r/acs/jacsat/~4/ak4BxkITHl8
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02-16-2012 05:24 AM
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies
Abstract Obtaining sequence-specific assignments remains a major bottleneck in solution NMR investigations of supramolecular structure, dynamics and interactions. Here we demonstrate that resonance assignment of methyl probes in high molecular weight protein assemblies can be efficiently achieved by combining fast NMR experiments, residue-type-specific isotope-labeling and automated site-directed mutagenesis. The utility of this general and straightforward strategy is demonstrated through...
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06-06-2011 12:53 AM
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
J Biomol NMR. 2011 May 29;
Authors: Amero C, Asunción Durá M, Noirclerc-Savoye M, Perollier A, Gallet B, Plevin MJ, Vernet T, Franzetti B, Boisbouvier J
Obtaining sequence-specific assignments remains a major bottleneck in solution NMR investigations of supramolecular structure, dynamics and interactions. Here we demonstrate that resonance...
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06-01-2011 02:30 PM
[NMR paper] NMR-driven discovery of benzoylanthranilic acid inhibitors of far upstream element bi
NMR-driven discovery of benzoylanthranilic acid inhibitors of far upstream element binding protein binding to the human oncogene c-myc promoter.
Related Articles NMR-driven discovery of benzoylanthranilic acid inhibitors of far upstream element binding protein binding to the human oncogene c-myc promoter.
J Med Chem. 2004 Sep 23;47(20):4851-7
Authors: Huth JR, Yu L, Collins I, Mack J, Mendoza R, Isaac B, Braddock DT, Muchmore SW, Comess KM, Fesik SW, Clore GM, Levens D, Hajduk PJ
Reversal of aberrant gene expression that is induced by the...
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11-24-2010 10:01 PM
[NMR paper] H-NMR study of temperature-induced structure alteration at the active site of horse h
H-NMR study of temperature-induced structure alteration at the active site of horse heart cytochrome c.
Related Articles H-NMR study of temperature-induced structure alteration at the active site of horse heart cytochrome c.
J Biochem. 1996 Jan;119(1):16-22
Authors: Yamamoto Y
The molecular structure of the active site of horse heart met-cyano cytochrome c, as a function of temperature, has been investigated using 1H-NMR. A temperature dependence study of the NMR spectra revealed that one heme methyl proton resonance exhibits anti-Curie...
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08-22-2010 02:27 PM
[NMR paper] 13C magic angle spinning NMR study of the light-induced and temperature-dependent cha
13C magic angle spinning NMR study of the light-induced and temperature-dependent changes in Rhodobacter sphaeroides R26 reaction centers enriched in tyrosine.
Related Articles 13C magic angle spinning NMR study of the light-induced and temperature-dependent changes in Rhodobacter sphaeroides R26 reaction centers enriched in tyrosine.
Biochemistry. 1992 Nov 17;31(45):11038-49
Authors: Fischer MR, de Groot HJ, Raap J, Winkel C, Hoff AJ, Lugtenburg J
Solid-state 13C magic angle spinning (MAS) NMR has been used to investigate...
Evidenceof Entropy-Driven Bistability through 15N NMR Analysisof a Temperature- and Solvent-Induced, ChiropticalSwitching Polycarbodiimide
Linear Mode
