[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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[NMR paper] Multidimensional NMR spectroscopy for protein characterization and assignment inside cells.
Multidimensional NMR spectroscopy for protein characterization and assignment inside cells.
Related Articles Multidimensional NMR spectroscopy for protein characterization and assignment inside cells.
J Am Chem Soc. 2005 Aug 10;127(31):10848-9
Authors: Reardon PN, Spicer LD
High-field, heteronuclear NMR spectroscopy of biological macromolecules in native cellular environments is limited by the low concentrations present and the long data acquisition times needed for the experiments. Successful 1D and 2D heteronuclear NMR data have been...
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[NMR paper] Evaluation of parameters critical to observing proteins inside living Escherichia col
Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy.
Related Articles Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy.
J Am Chem Soc. 2001 Sep 19;123(37):8895-901
Authors: Serber Z, Ledwidge R, Miller SM, Dötsch V
Our recently developed in-cell NMR procedure now enables one to observe protein conformations inside living cells. Optimization of the technique demonstrates that distinguishing the signals produced by a...
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[NMR paper] Reaction of cis- and trans-[PtCl2(NH3)2] with reduced glutathione inside human red bl
Reaction of cis- and trans- with reduced glutathione inside human red blood cells, studied by 1H and 15N- DEPT NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Reaction of cis- and trans- with reduced glutathione inside human red blood cells, studied by 1H and 15N- DEPT NMR.
J Inorg Biochem. 1990 Apr;38(4):327-45
Authors: Berners-Price SJ, Kuchel PW
Reactions of cis- and trans- with glutathione (GSH) inside intact red blood cells have been studied by 1H spin-echo...