'Sweet' quantum dots light the way for new HIV and Ebola treatment Nanowerk
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. A new academic symposium, the Asbury ...
'Sweet' quantum dots light the way for new HIV and Ebola treatment - Nanowerk More...
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Building better bilayers - Nanowerk
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Building better bilayers
Nanowerk
These bicelles are then analyzed using a technique called nuclear magnetic resonance spectroscopy. In this technique, the proteins under investigation are exposed to a magnetic field that causes them to spontaneously align, enabling detailed structural ...
Building better bilayers - Nanowerk
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Structure of Colloidal Quantum Dots from Dynamic Nuclear Polarization Surface Enhanced NMR Spectroscopy
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Structureof Colloidal Quantum Dots from Dynamic NuclearPolarization Surface Enhanced NMR Spectroscopy
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http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b09248/20151023/images/medium/ja-2015-09248y_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b09248
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
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12-06-2014 04:54 AM
Dynamic nuclear polarization and Hanle effect in (In,Ga)As/GaAs quantum dots. Role of nuclear spin fluctuations
From The DNP-NMR Blog:
Dynamic nuclear polarization and Hanle effect in (In,Ga)As/GaAs quantum dots. Role of nuclear spin fluctuations
Gerlovin, I.Y., et al., Dynamic nuclear polarization and Hanle effect in (In,Ga)As/GaAs quantum dots. Role of nuclear spin fluctuations. AIP Conference Proceedings, 2013. 1566(1): p. 319-320.
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06-06-2014 03:59 PM
A trick to fold proteins more quickly - Nanowerk - Nanowerk
A trick to fold proteins more quickly - Nanowerk - Nanowerk
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A trick to fold proteins more quickly - Nanowerk
Nanowerk
... to create restraints to be applied to the modelâ??, explained Laio, who has coordinated the research published in Proceedings of the National Academy of Sciences ("Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics").
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