ProteinDielectric Constants Determined from NMR ChemicalShift Perturbations
ProteinDielectric Constants Determined from NMR ChemicalShift Perturbations
Predrag Kukic, Damien Farrell, Lawrence P. McIntosh, Bertrand Garci?a-Moreno E., Kristine Steen Jensen, Zigmantas Toleikis, Kaare Teilum and Jens Erik Nielsen
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja406995j/aop/images/medium/ja-2013-06995j_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja406995j
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
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[NMR paper] Protein Dielectric Constants Determined from NMR Chemical Shift Perturbations.
Protein Dielectric Constants Determined from NMR Chemical Shift Perturbations.
Protein Dielectric Constants Determined from NMR Chemical Shift Perturbations.
J Am Chem Soc. 2013 Oct 14;
Authors: Kukic P, Farrell D, McIntosh LP, Garcia-Moreno E B, Jensen KS, Toleikis Z, Teilum K, Nielsen JE
Abstract
Understanding the connection between protein structure and function requires a quantitative understanding of electrostatic effects. Structure-based electrostatics calculations are essential for this purpose, but their use have been limited by a...
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10-16-2013 11:22 AM
Liouvillians in NMR: The direct method revisited
Liouvillians in NMR: The direct method revisited
October 2011
Publication year: 2011
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 59, Issue 3</br>
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12-15-2012 09:51 AM
Measurement of rate constants for homodimer subunit exchange using double electronâ??electron resonance and paramagnetic relaxation enhancements
Measurement of rate constants for homodimer subunit exchange using double electronâ??electron resonance and paramagnetic relaxation enhancements
Abstract Here, we report novel methods to measure rate constants for homodimer subunit exchange using double electronâ??electron resonance (DEER) electron paramagnetic resonance spectroscopy measurements and nuclear magnetic resonance spectroscopy based paramagnetic relaxation enhancement (PRE) measurements. The techniques were demonstrated using the homodimeric protein Dsy0195 from the strictly anaerobic bacterium Desulfitobacterium...
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A study on the influence of fast amide exchange on the accuracy of 15N relaxation rate constants
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Abstract 15N relaxation rates of amide moieties provide insight both into global as well as local backbone dynamics of peptides and proteins. As the differences in the relaxation rates in general are small, their accurate determination is of prime importance. One potential source of error is fast amide exchange. It is well known that in its presence the effects of saturation transfer and H/D exchange may result in erroneous apparent relaxation rates R 1 and R 2. Here, the extent of...
Increased precision for analysis of proteinâ??ligand dissociation constants determined from chemical shift titrations
Increased precision for analysis of proteinâ??ligand dissociation constants determined from chemical shift titrations
Abstract NMR is ideally suited for the analysis of proteinâ??protein and protein ligand interactions with dissociation constants ranging from ~2 ÎĽM to ~1 mM, and with kinetics in the fast exchange regime on the NMR timescale. For the determination of dissociation constants (K D ) of 1:1 proteinâ??protein or proteinâ??ligand interactions using NMR, the protein and ligand concentrations must necessarily be similar in magnitude to the K D , and nonlinear least squares...
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05-01-2012 07:06 AM
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Binding affinity difference induced by the stereochemistry of the sulfoxide bridge of the cyclic peptide inhibitors of Grb2-SH2 domain: NMR studies for the structural origin.
Related Articles Binding affinity difference induced by the stereochemistry of the sulfoxide bridge of the cyclic peptide inhibitors of Grb2-SH2 domain: NMR studies for the structural origin.
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The SAR study on a phage library-derived...