New catalysts containing antimony could complement more well-known interactions such as hydrogen bonds or chalcogen-sulfur bonds in chemical reactions for a wide range of products. Nuclear magnetic resonance (NMR) spectroscopy provides the clues.
Application of the Halogen Bond in Protein Systems
Application of the Halogen Bond in Protein Systems
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00371/20170523/images/medium/bi-2017-00371y_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00371
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05-24-2017 06:27 AM
Structure–Energy Relationships of Halogen Bonds in Proteins
Structure–Energy Relationships of Halogen Bonds in Proteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00022/20170407/images/medium/bi-2017-000223_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00022
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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04-22-2017 10:30 PM
Anemones punch holes: Toxins by NMR
Anemones punch holes: Toxins by NMR
http://www.spectroscopynow.com/common/images/thumbnails/15b1e53c8f5.jpgA new approach to constructing a sea anemone toxin makes it plausible to incorporate site-specific isotopic labels for solid-state nuclear magnetic resonance (NMR) spectroscopic structural studies that will ultimately reveal how it functions and provide clues as to the action of other pore-forming proteins.
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04-01-2017 02:53 AM
Useof 77Se and 125Te NMR Spectroscopyto Probe Covalency of the Actinide-Chalcogen Bonding in [Th(En){N(SiMe3)2}3]- (E = Se, Te; n = 1, 2) andTheir Oxo-Uranium(VI) Congeners
Useof 77Se and 125Te NMR Spectroscopyto Probe Covalency of the Actinide-Chalcogen Bonding in - (E = Se, Te; n = 1, 2) andTheir Oxo-Uranium(VI) Congeners
Danil E. Smiles, Guang Wu, Peter Hroba?rik and Trevor W. Hayton
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b07767/20160111/images/medium/ja-2015-07767u_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b07767
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http://feeds.feedburner.com/~r/acs/jacsat/~4/EV2sHQnPe0s
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01-13-2016 04:53 AM
StructuralBasis of the Green–Blue Color Switchingin Proteorhodopsin as Determined by NMR Spectroscopy
StructuralBasis of the Green–Blue Color Switchingin Proteorhodopsin as Determined by NMR Spectroscopy
Jiafei Mao, Nhu-Nguyen Do, Frank Scholz, Lenica Reggie, Michaela Mehler, Andrea Lakatos, Yean-Sin Ong, Sandra J. Ullrich, Lynda J. Brown, Richard C. D. Brown, Johanna Becker-Baldus, Josef Wachtveitl and Clemens Glaubitz
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja5097946/20141204/images/medium/ja-2014-097946_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja5097946...
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12-05-2014 07:30 AM
Why Are Lobsters Blue, and Why Does Cooking Turn Them Red? - New York Times
<img alt="" height="1" width="1" />
Why Are Lobsters Blue, and Why Does Cooking Turn Them Red?
New York Times
... the wavelengths of light that are absorbed. Using nuclear magnetic resonance imaging and spectroscopy to examine protein-pigment interactions, the researchers found that this effect was a large one, suggesting that it is the primary source of ...
Why Are Lobsters Blue, and Why Does Cooking Turn Them Red? - New York Times
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09-17-2013 08:35 AM
[NMR900 blog] CSC 2013 symposium - "Halogen Bonding and other Non-Covalent Interactions"
CSC 2013 symposium - "Halogen Bonding and other Non-Covalent Interactions"
David Bryce (Ottawa) and Mark Taylor (Toronto) are organizing a symposium on "Halogen Bonding and other Non-Covalent Interactions" to be held as part of the Canadian Chemistry Conference in Quebec City, May 26-30, 2013. International experts including Prof. Pierangelo Metrangolo (Milan, Italy), Prof. Giuseppe Resnati (Milan, Italy), Prof. P. Shing Ho (Colorado State, USA), and Prof. Duncan Bruce (York, UK) have already agreed to give oral presentations at the meeting. Although this is not an NMR-focussed symposium,...
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10-22-2012 09:07 PM
[NMR paper] A simple protocol to study blue copper proteins by NMR.
A simple protocol to study blue copper proteins by NMR.
Related Articles A simple protocol to study blue copper proteins by NMR.
Eur J Biochem. 2003 Feb;270(4):600-9
Authors: Gelis I, Katsaros N, Luchinat C, Piccioli M, Poggi L
In the case of oxidized plastocyanin from Synechocystis sp. PCC6803, an NMR approach based on classical two and three dimensional experiments for sequential assignment leaves unobserved 14 out of 98 amino acids. A protocol which simply makes use of tailored versions of 2D HSQC and 3D CBCA(CO)NH and CBCANH leads to the...
Pnictogen, chalcogen, halogen: NMR looks into the blue holes
New catalysts containing antimony could complement more well-known interactions such as hydrogen bonds or chalcogen-sulfur bonds in chemical reactions for a wide range of products. Nuclear magnetic resonance (NMR) spectroscopy provides the clues.
Linear Mode
