Related ArticlesIdentification of protein surfaces by NMR measurements with a pramagnetic Gd(III) chelate.
J Am Chem Soc. 2002 Jan 23;124(3):372-3
Authors: Pintacuda G, Otting G
Gd-diethylenetriamine pentaacetic acid-bismethylamide, Gd(DTPA-BMA), is shown to be a reagent suitable for the identification of protein surfaces. Compared to the conventionally used spin-label TEMPOL, Gd(DTPA-BMA) is a stronger relaxation agent, requiring lesser concentrations to achieve the same paramagnetic relaxation enhancement of solvent-exposed protein protons. It is also less hydrophobic and therefore less prone to specific binding to proteins. Relaxation enhancements predicted by a second-sphere interaction model correlated with experimental data recorded with ubiquitin, while the correlation with corresponding data recorded with TEMPOL was poor.
Structure of Peptides on Metal Oxide Surfaces Probed by NMR
Structure of Peptides on Metal Oxide Surfaces Probed by NMR
Peter A. Mirau, Rajesh R. Naik and Patricia Gehring
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja205454t/aop/images/medium/ja-2011-05454t_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja205454t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/twbT3VIr8Xo
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Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
J Struct Biol. 2011 Apr 9;
Authors: Kodama Y, Reese ML, Shimba N, Ono K, Kanamori E, Dötsch V, Noguchi S, Fukunishi Y, Suzuki EI, Shimada I, Takahashi H
Protein-protein interactions are necessary for various cellular...
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Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Angew Chem Int Ed Engl. 2011 Mar 18;
Authors: Salmon L, Ortega Roldan JL, Lescop E, Licinio A, van Nuland N, Jensen MR, Blackledge M
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[NMR paper] Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Related Articles Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Protein Pept Lett. 2005 Apr;12(3):235-40
Authors: Spyracopoulos L
Protein dynamics and thermodynamics can be characterized through measurements of relaxation rates of side chain (2)H and (13)C, and backbone (15)N nuclei using NMR spectroscopy. The rates reflect protein motions on timescales from picoseconds to milliseconds. Backbone and methyl side chain NMR...
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[NMR paper] Protein dynamics measurements by TROSY-based NMR experiments.
Protein dynamics measurements by TROSY-based NMR experiments.
Related Articles Protein dynamics measurements by TROSY-based NMR experiments.
J Magn Reson. 2000 Apr;143(2):423-6
Authors: Zhu G, Xia Y, Nicholson LK, Sze KH
The described TROSY-based experiments for investigating backbone dynamics of proteins make it possible to elucidate internal motions in large proteins via measurements of T(1), T(2), and NOE of backbone (15)N nuclei. In our proposed sequences, the INEPT sequence is eliminated and the PEP sequence is replaced by the ST2-PT...
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[NMR paper] Exploring surfaces and cavities in lipoxygenase and other proteins by hyperpolarized
Exploring surfaces and cavities in lipoxygenase and other proteins by hyperpolarized xenon-129 NMR.
Related Articles Exploring surfaces and cavities in lipoxygenase and other proteins by hyperpolarized xenon-129 NMR.
J Am Chem Soc. 1999 Oct 13;121(40):9370-7
Authors: Bowers CR, Storhaug V, Webster CE, Bharatam J, Cottone A, Gianna R, Betsey K, Gaffney BJ
This paper presents an exploratory study of the binding interactions of xenon with the surface of several different proteins in the solution and solid states using both conventional and...
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[NMR paper] NMR identification of protein surfaces using paramagnetic probes.
NMR identification of protein surfaces using paramagnetic probes.
Related Articles NMR identification of protein surfaces using paramagnetic probes.
Biochemistry. 1990 Oct 30;29(43):10041-8
Authors: Petros AM, Mueller L, Kopple KD
Paramagnetic agents produce line broadening and thus cancellation of anti phase cross-peak components in two-dimensional correlated nuclear magnetic resonance spectra. The specificity of this effect was examined to determine its utility for identifying surface residues of proteins. Ubiquitin and hen egg white...
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[NMR paper] NMR studies of protein surfaces. The interaction of lysozyme with tri-N-acetylglucosa
NMR studies of protein surfaces. The interaction of lysozyme with tri-N-acetylglucosamine.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of protein surfaces. The interaction of lysozyme with tri-N-acetylglucosamine.
Biochem Pharmacol. 1990 Jul 1;40(1):65-8
Authors: Petros AM, Kopple KD
Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) che
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