Related ArticlesIdentification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy.
Molecules. 2015;20(12):21992-9
Authors: Ferrage F, Dutta K, Cowburn D
Abstract
The proper characterization of protein-ligand interfaces is essential for structural biology, with implications ranging from the fundamental understanding of biological processes to pharmacology. Nuclear magnetic resonance is a powerful technique for such studies. We propose a novel approach to the direct determination of the likely pose of a peptide ligand onto a protein partner, by using frequency-selective cross-saturation with a low stringency isotopic labeling methods. Our method illustrates a complex of the Src homology 3 domain of C-terminal Src kinase with a peptide from the proline-enriched tyrosine phosphatase.
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
J Biol Inorg Chem. 2011 Apr 3;
Authors: Teixeira JM, Dias DM, Cañada FJ, Martins JA, André JP, Jiménez-Barbero J, Geraldes CF
The study of ligand-receptor interactions using high-resolution NMR techniques, namely the saturation transfer difference (STD),...
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Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Methods Enzymol. 2011;493:241-75
Authors: Ziarek JJ, Peterson FC, Lytle BL, Volkman BF
Over the last 15years, the role of NMR spectroscopy in the lead identification and optimization stages of pharmaceutical drug discovery has steadily increased. NMR occupies a unique niche in the biophysical analysis of drug-like...
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[NMR paper] Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Related Articles Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
J Am Chem Soc. 2005 Sep 28;127(38):13110-1
Authors: Soubias O, Gawrisch K
We studied the interaction of mono- and polyunsaturated phosphatidylcholines with rhodopsin by 1H NMR saturation transfer difference spectroscopy with magic angle spinning (STD-MAS NMR). The results indicate a strong preference for interaction of rhodopsin with the...
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[NMR paper] NMR identification of hydrophobic cavities with low water occupancies in protein stru
NMR identification of hydrophobic cavities with low water occupancies in protein structures using small gas molecules.
Related Articles NMR identification of hydrophobic cavities with low water occupancies in protein structures using small gas molecules.
Nat Struct Biol. 1997 May;4(5):396-404
Authors: Otting G, Liepinsh E, Halle B, Frey U
Magnetization transfer through dipole-dipole interactions (nuclear Overhauser effects, NOEs) between water protons and the protons lining two small hydrophobic cavities in hen egg-white lysozyme demonstrates...
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[NMR paper] NMR identification of hydrophobic cavities with low water occupancies in protein stru
NMR identification of hydrophobic cavities with low water occupancies in protein structures using small gas molecules.
Related Articles NMR identification of hydrophobic cavities with low water occupancies in protein structures using small gas molecules.
Nat Struct Biol. 1997 May;4(5):396-404
Authors: Otting G, Liepinsh E, Halle B, Frey U
Magnetization transfer through dipole-dipole interactions (nuclear Overhauser effects, NOEs) between water protons and the protons lining two small hydrophobic cavities in hen egg-white lysozyme demonstrates...
Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy.
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