Nuclear magnetic resonance (NMR) (15)N relaxation measurements of the olfactory marker protein (OMP) including longitudinal relaxation (T(1)), transverse relaxation (T(2)), and (15)N-{(1)H} NOE data were collected at low protein concentrations (
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Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
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Top Curr Chem. 2011 Sep 7;
Authors: Ishima R
Abstract
Nuclear Magnetic Resonance (NMR) relaxation is a powerful technique that provides information about internal dynamics associated with configurational energetics in proteins, as well as site-specific information involved in conformational equilibria. In particular, (15)N relaxation is a useful probe to...
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[NMR paper] Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
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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] Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implicati
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The melanoma inhibitory activity (MIA) protein is a clinically valuable marker in patients with malignant melanoma as enhanced values diagnose metastatic...
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[NMR paper] Main-chain dynamics of a partially folded protein: 15N NMR relaxation measurements of
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J Mol Biol. 1996 Apr 5;257(3):669-83
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15N NMR relaxation measurements have been used to study the dynamic...
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[NMR paper] Backbone dynamics of trp repressor studied by 15N NMR relaxation.
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Backbone dynamics of trp repressor, a 25 kDa DNA binding protein, have been studied using 15N relaxation data measured by proton-detected two-dimensional 1H-15N NMR spectroscopy. 15N spin-lattice relaxation time (T1), spin-spin relaxation time (T2), and heteronuclear NOEs were determined for all visible backbone...
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Backbone dynamics of the major tacrolimus (FK506) binding protein (FKBP-12, 107 amino acids) have been studied using 15N relaxation data derived from proton-detected two-dimensional 1H-15N NMR spectroscopy....
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J Magn Reson. 1999 Jun;138(2):244-55
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Superslow backbone dynamics of the protein barstar and the polypeptide polyglycine was studied by...