Protein cavities often rely on the paramagnetic metal present in their active site in order to catalyse various chemical transformations in biology. The selective detection and identification of the substrate is of fundamental importance in environmental monitoring and biological studies. Herein, a covalently linked Fe(iii)porphyrin dimer-based paramagnetic sensory cavity has been devised for the accurate detection and simultaneous identification of phenol (substrate) binding within the cavity...
[ASAP] Triple Resonance Experiments for the Rapid Detection of 103Rh NMR Shifts: A Combined Experimental and Theoretical Study into Dirhodium and Bismuth–Rhodium Paddlewheel Complexes
Triple Resonance Experiments for the Rapid Detection of 103Rh NMR Shifts: A Combined Experimental and Theoretical Study into Dirhodium and Bismuth–Rhodium Paddlewheel Complexes
Fabio P. Calo?, Giovanni Bistoni, Alexander A. Auer, Markus Leutzsch, and Alois Fu?rstner
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.1c06414/20210804/images/medium/ja1c06414_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.1c06414
http://feeds.feedburner.com/~r/acs/jacsat/~4/-hX522JCXMI
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08-05-2021 05:28 PM
[NMR paper] Computational approaches to amino acid side-chain conformation using combined NMR theoretical and experimental results: leucine-67 in Desulfovibrio vulgaris flavodoxin
Computational approaches to amino acid side-chain conformation using combined NMR theoretical and experimental results: leucine-67 in Desulfovibrio vulgaris flavodoxin
In this paper, we show that the combination of NMR theoretical and experimental results can help to solve the molecular structure of peptides, here it is used as an example the residue Leucine-67 in Desulfovibrio vulgaris flavodoxin. We apply a computational protocol based on the leucine amino acid dipeptide, which, using calculated and experimental spin-spin coupling constants, allows us to obtain the conformation of the...
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02-24-2021 05:50 AM
[NMR paper] Computational approaches to amino acid side-chain conformation using combined NMR theoretical and experimental results: leucine-67 in Desulfovibrio vulgaris flavodoxin.
Computational approaches to amino acid side-chain conformation using combined NMR theoretical and experimental results: leucine-67 in Desulfovibrio vulgaris flavodoxin.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--academic.oup.com-images-oup_pubmed.png Related Articles Computational approaches to amino acid side-chain conformation using combined NMR theoretical and experimental results: leucine-67 in Desulfovibrio vulgaris flavodoxin.
Brief Bioinform. 2021 Feb 11;:
Authors: San Fabián J, Omar S, García de la Vega JM
...
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02-15-2021 01:33 PM
Coherent evolution of parahydrogen induced polarisation using laser pump, NMR probe spectroscopy: Theoretical framework and experimental observation
From The DNP-NMR Blog:
Coherent evolution of parahydrogen induced polarisation using laser pump, NMR probe spectroscopy: Theoretical framework and experimental observation
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Halse, M.E., et al., Coherent evolution of parahydrogen induced polarisation using laser pump, NMR probe spectroscopy: Theoretical framework and experimental observation. J Magn Reson, 2017. 278: p. 25-38.
https://www.ncbi.nlm.nih.gov/pubmed/28347906
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07-20-2017 08:40 AM
[NMR paper] Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Proc Natl Acad Sci U S A. 2013 Jun 24;
Authors: Libich DS, Fawzi NL, Ying J, Clore GM
Abstract
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06-27-2013 02:10 PM
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
J Inorg Biochem. 2010 Oct;104(10):1063-70
Authors: Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN
Proton 2D NMR was used to confirm in solution a highly conserved portion of the molecular structure upon substrate loss for the...
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02-10-2011 03:51 PM
[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...
Probing substrate binding inside a paramagnetic cavity: a NMR spectroscopy toolbox for combined experimental and theoretical investigation
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