Nuclear magnetic resonance (NMR) spectroscopy has been used to reveal the three-dimensional structure of the copL protein in the Bacillus subtilis bacterium, a close relative of Staphylococcus aureus. The approach reveals copper ions can bind to the surface of the protein and points to how resistance to this antibacterial agent can arise.
Stony coral: NMR and climate resistance
Stony coral: NMR and climate resistance
http://www.spectroscopynow.com/common/images/thumbnails/15ca0b1cc7b.jpg2D nuclear magnetic resonance (NMR) spectroscopy and ultra-high-resolution 3D imaging have been used to investigate a well-known and previously well-studied stony coral of the Indo-Pacific to reveal that it precipitates minerals through a biologically driven process. The findings suggest that this particular species may be more resistant to climate change than first thought.
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06-15-2017 03:26 AM
Reversing resistance: Rose myrtle extracts analysed by NMR
Reversing resistance: Rose myrtle extracts analysed by NMR
http://www.spectroscopynow.com/common/images/thumbnails/15a8479edab.jpgNovel natural products found in rose myrtle could hold promise of a new way to make breast cancer cells that have become resistant to the conventional anticancer drug doxorubicin susceptible once more. Nuclear magnetic resonance (NMR) spectroscopy, electronic circular dichroism (ECD) and X-ray crystallography were used to determine the structures and absolute configurations of the compounds.
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03-01-2017 05:04 PM
Unravelling the secret of antibiotic resistance - Phys.Org
http://www.bionmr.com//t0.gstatic.com/images?q=tbn:ANd9GcQrSW_2Js0UxyV4CKAVBlZwuQU3gD2nd4WXI7Rz-VO4kgsMKKSJUj3BnyqIwVZVpRpayifLXFM
Phys.Org
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Unravelling the secret of antibiotic resistance
Phys.Org
A recent £17 million investment in some of the best nuclear magnetic resonance and electron microscopy facilities in the world is now enabling scientists to remain at the forefront of research into complex proteins. The University of Leeds has played a ...
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Unravelling the secret of antibiotic resistance - Phys.Org
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03-25-2016 04:12 PM
Elusive Transmetalation Intermediate in Copper-Catalyzed Conjugate Additions: Direct NMR Detection of an Ethyl Group Attached to a Binuclear Phosphoramidite Copper Complex
Elusive Transmetalation Intermediate in Copper-Catalyzed Conjugate Additions: Direct NMR Detection of an Ethyl Group Attached to a Binuclear Phosphoramidite Copper Complex
Felicitas von Rekowski, Carina Koch and Ruth M. Gschwind
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja504577t/aop/images/medium/ja-2014-04577t_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja504577t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/V2rZJxvuMXQ
nmrlearner
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08-02-2014 12:38 PM
[NMR paper] A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
Related Articles A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
J Biol Chem. 2005 Nov 18;280(46):38259-63
Authors: Banci L, Bertini I, Cantini F, Chasapis CT, Hadjiliadis N, Rosato A
ATP7A is a P-type ATPase involved in copper(I) homeostasis in humans. It possesses a long N-terminal tail protruding into the cytosol and containing six...
nmrlearner
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12-01-2010 06:56 PM
[NMR paper] Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study.
Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study.
Related Articles Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study.
Anal Bioanal Chem. 2004 Aug;379(7-8):1045-9
Authors: Nissler L, Gebhardt R, Berger S
Flavonoids are well known to inhibit the function of the multi-drug-resistance (mdr) transporter by interacting with their ATP binding domains. The precise orientation of these molecules inside the ATP binding pocket is still unclear. We applied the saturation transfer...
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11-24-2010 09:51 PM
[NMR paper] Differentiation of the P-gp and MRP1 multidrug resistance systems by mobile lipid 1H-
Differentiation of the P-gp and MRP1 multidrug resistance systems by mobile lipid 1H-NMR spectroscopy and phosphatidylserine externalization.
Related Articles Differentiation of the P-gp and MRP1 multidrug resistance systems by mobile lipid 1H-NMR spectroscopy and phosphatidylserine externalization.
Anticancer Res. 2001 Nov-Dec;21(6A):3915-9
Authors: Mannechez A, Collet B, Payen L, Lecureur V, Fardel O, Le Moyec L, de Certaines JD, Leray G
We have previously demonstrated that proton NMR spectra of fatty acid chains in erythroleukemia K562...
Staph fights copper: NMR and resistance
Nuclear magnetic resonance (NMR) spectroscopy has been used to reveal the three-dimensional structure of the copL protein in the Bacillus subtilis bacterium, a close relative of Staphylococcus aureus. The approach reveals copper ions can bind to the surface of the protein and points to how resistance to this antibacterial agent can arise.
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