[NMR paper] Structural Analysis of Protein-RNA Complexes in Solution Using NMR Paramagnetic Relaxation Enhancements.
Structural Analysis of Protein-RNA Complexes in Solution Using NMR Paramagnetic Relaxation Enhancements.
Related Articles Structural Analysis of Protein-RNA Complexes in Solution Using NMR Paramagnetic Relaxation Enhancements.
Methods Enzymol. 2015;558:333-362
Authors: Hennig J, Warner LR, Simon B, Geerlof A, Mackereth CD, Sattler M
Abstract
Biological activity in the cell is predominantly mediated by large multiprotein and protein-nucleic acid complexes that act together to ensure functional fidelity. Nuclear magnetic resonance...
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06-13-2015 11:09 PM
[NMR paper] NMR approaches for structural analysis of multidomain proteins and complexes in solution.
NMR approaches for structural analysis of multidomain proteins and complexes in solution.
Related Articles NMR approaches for structural analysis of multidomain proteins and complexes in solution.
Prog Nucl Magn Reson Spectrosc. 2014 Jul;80C:26-63
Authors: Göbl C, Madl T, Simon B, Sattler M
Abstract
NMR spectroscopy is a key method for studying the structure and dynamics of (large) multidomain proteins and complexes in solution. It plays a unique role in integrated structural biology approaches as especially information about...
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NMR approaches for structural analysis of multidomain proteins and complexes in solution
NMR approaches for structural analysis of multidomain proteins and complexes in solution
Publication date: Available online 23 May 2014
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Christoph Göbl , Tobias Madl , Bernd Simon , Michael Sattler</br>
NMR spectroscopy is a key method for studying the structure and dynamics of (large) multidomain proteins and complexes in solution. It plays a unique role in integrated structural biology approaches as especially information about conformational dynamics can be readily obtained at residue...
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05-23-2014 03:21 PM
Nature and Structure of Aluminum Surface Sites Grafted on Silica from a Combination of High-Field Aluminum-27 Solid-State NMR Spectroscopy and First-Principles Calculations
Nature and Structure of Aluminum Surface Sites Grafted on Silica from a Combination of High-Field Aluminum-27 Solid-State NMR Spectroscopy and First-Principles Calculations
Rachel Nathaniel Kerber, Anthony Kermagoret, Emmanuel Callens, Pierre Florian, Dominique Massiot, Anne Lesage, Christophe Cope?ret, Franc?oise Delbecq, Xavier Rozanska and Philippe Sautet
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja3008566/aop/images/medium/ja-2012-008566_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja3008566
...
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04-10-2012 02:44 AM
[NMR paper] 31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes
31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes.
Related Articles 31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes.
Eur J Biochem. 2000 Feb;267(4):1223-9
Authors: Castagné C, Murphy EC, Gronenborn AM, Delepierre M
Complexes of the HMG box protein SRY with two duplexes of 8 and 14 base pairs have been studied by 31P NMR and complete assignment of all phosphorus signals of the bound DNA duplexes are presented. While for the free DNA, all 31P signals display limited...
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[NMR paper] NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou
NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Related Articles NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Biochemistry. 1994 Jan 25;33(3):644-50
Authors: Fraenkel Y, Gershoni JM, Navon G
A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a...
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08-22-2010 03:33 AM
[NMR paper] NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou
NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Related Articles NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Biochemistry. 1994 Jan 25;33(3):644-50
Authors: Fraenkel Y, Gershoni JM, Navon G
A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a...
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08-22-2010 03:33 AM
[NMR paper] Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical a
Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculations.
Related Articles Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculations.
Biochemistry. 1993 Jan 12;32(1):282-9
Authors: Adler M, Carter P, Lazarus RA, Wagner G
The pairing of the cysteines in disulfide bonds was investigated for the 68-residue RGD-containing protein kistrin, a potent antagonist of the integrin GP IIbIIIa and an inhibitor of platelet...