Related ArticlesXenon-Protein Interactions: Characterization by X-Ray Crystallography and Hyper-CEST NMR.
Methods Enzymol. 2018;602:249-272
Authors: Roose BW, Zemerov SD, Dmochowski IJ
Abstract
The physiological activity of xenon has long been recognized, though the exact nature of its interactions with biomolecules remains poorly understood. Xe is an inert noble gas, but can act as a general anesthetic, most likely by binding internal hydrophobic cavities within proteins. Understanding Xe-protein interactions, therefore, can provide crucial insight regarding the mechanism of Xe anesthesia and potentially other general anesthetic agents. Historically, Xe-protein interactions have been studied primarily through X-ray crystallography and nuclear magnetic resonance (NMR). In this chapter, we first describe our methods for preparing Xe derivatives of protein crystals and identifying Xe-binding sites. Second, we detail our procedure for 129Xe hyper-CEST NMR spectroscopy, a versatile NMR technique well suited for characterizing the weak, transient nature of Xe-protein interactions.
A new class of CEST experiment based on selecting different magnetization components at the start and end of the CEST relaxation element: an application to 1 H CEST
A new class of CEST experiment based on selecting different magnetization components at the start and end of the CEST relaxation element: an application to 1 H CEST
Abstract
Chemical exchange saturation transfer (CEST) experiments are becoming increasingly popular for investigating biomolecular exchange dynamics with rates on the order of approximately 50â??500Â*sâ??1 and a rich toolkit of different methods has emerged over the past few years. Typically, experiments are based on the evolution of longitudinal magnetization, or in some cases two-spin...
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01-19-2018 08:57 PM
[NMR paper] Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.
Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.
Related Articles Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.
Methods Mol Biol. 2017;1588:143-156
Authors: Grondin JM, Langelaan DN, Smith SP
Abstract
Solution-state nuclear magnetic resonance (NMR) spectroscopy can be used to monitor protein-carbohydrate interactions. Two-dimensional (1)H-(15)N heteronuclear single quantum coherence (HSQC)-based techniques described in this chapter can be used quickly and effectively to...
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04-19-2017 01:07 PM
Using ITC Technique for Characterization of Protein-Protein Interactions - News-Medical.net
Using ITC Technique for Characterization of Protein-Protein Interactions - News-Medical.net
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Using ITC Technique for Characterization of Protein-Protein Interactions
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With each interaction, the protein structural changes occur through specific electrostatic and van der Waals interactions, the breaking and formation of hydrogen bonds and the burial of surfaces exposed to solvents. It is...
[NMR paper] Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
Related Articles Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
J Am Chem Soc. 2005 Aug 24;127(33):11676-83
Authors: Desvaux H, Dubois L, Huber G, Quillin ML, Berthault P, Matthews BW
Wild-type bacteriophage T4 lysozyme contains a hydrophobic cavity with binding properties that have been...
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12-01-2010 06:56 PM
[NMR paper] Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectr
Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectroscopy.
Related Articles Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectroscopy.
J Mol Biol. 2002 Sep 13;322(2):425-40
Authors: Rubin SM, Lee SY, Ruiz EJ, Pines A, Wemmer DE
Xenon-binding sites in proteins have led to a number of applications of xenon in biochemical and structural studies. Here we further develop the utility of 129Xe NMR in characterizing specific xenon-protein interactions. The sensitivity of the 129Xe...
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11-24-2010 08:58 PM
[NMR paper] HYPER: a hierarchical algorithm for automatic determination of protein dihedral-angle
HYPER: a hierarchical algorithm for automatic determination of protein dihedral-angle constraints and stereospecific C beta H2 resonance assignments from NMR data.
Related Articles HYPER: a hierarchical algorithm for automatic determination of protein dihedral-angle constraints and stereospecific C beta H2 resonance assignments from NMR data.
J Biomol NMR. 1999 Nov;15(3):251-64
Authors: Tejero R, Monleon D, Celda B, Powers R, Montelione GT
A new computer program, HYPER, has been developed for automated analysis of protein dihedral angle values...
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11-18-2010 08:31 PM
Postdoctoral position to study Protein-Protein Interactions and their role in Mechanisms of Signal Transduction using protein solution NMR/x-ray crystallography
Spincore.com are advertising a postdoc NMR position. It sounds pretty interesting.
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Postdoctoral position to study Protein-Protein Interactions and their role in Mechanisms of Signal Transduction using protein solution NMR /x-ray crystallography
Case Medical School, Cleveland, Ohio, USA
How are signaling events transmitted from one protein to another? To answer this question we are looking to add a postdoctoral co-workers to our interdisciplinary team. Our interest is to understand protein-protein interactions, protein structure and dynamics in the context of cell signaling...
Xenon-Protein Interactions: Characterization by X-Ray Crystallography and Hyper-CEST NMR.
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