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Klaas Wynne
41 followers -
Chemical physicist and hill runner
Chemical physicist and hill runner

41 followers
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Long-standing controversy over the liquid-liquid transition in super-cooled n-butanol solved. Turns out that the new phase is a liquid crystal but one that is not simply in-between the liquid and the crystal. This leads to unusual properties not normally seen in liquid crystals. This result has implications for understanding super-cooling and glass formation in general.

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Our paper "Observation of coherent delocalized phonon-like modes in DNA under physiological conditions" just came out in Nature Communications. Go ahead and download for free (we paid $5000 for it) at http://www.nature.com/ncomms/2016/160601/ncomms11799/full/ncomms11799.html

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Paper just out in JPCLett "Order Parameter of the Liquid–Liquid Transition in a Molecular Liquid" http://pubs.acs.org/doi/abs/10.1021/jz5022763. Firstt application of fluorescence lifetime imaging (FLIM) to a condensed matter problem (liquid-liquid transitions)
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A simple description of our paper in icy water fluff in ChemComm http://pubs.rsc.org/en/content/articlelanding/2014/cc/c4cc07880b#!divAbstract plus a link to a YouTube movie showing live growing fluff.

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Low-frequency collective vibrational modes in proteins have been proposed as being responsible for efficiently directing biochemical reactions and biological energy transport. However, evidence of the existence of delocalized vibrational modes is scarce and proof of
their involvement in biological function absent. Here we apply extremely sensitive femtosecond optical Kerr-effect spectroscopy to study the depolarized Raman spectra of lysozyme and its complex with the inhibitor triacetylchitotriose in solution. Underdamped delocalized vibrational modes in the terahertz frequency domain are identified and shown to blue-shift and strengthen upon inhibitor binding. This demonstrates that the ligand-binding coordinate in proteins is underdamped and not simply solvent-controlled as previously assumed. The presence of such underdamped delocalized modes in proteins may have significant implications for the understanding of the efficiency of ligand binding and protein–molecule interactions, and has wider implications for biochemical reactivity and biological function.

http://www.nature.com/ncomms/2014/140603/ncomms4999/full/ncomms4999.html
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