Decoding 'sweet codes' that determine protein fates

Monday, September 15, 2014 - 08:00 in Physics & Chemistry

We often experience difficulties in identifying the accurate shape of dynamic and fluctuating objects. This is especially the case in the nanoscale world of biomolecules. The research group lead by Professor Koichi Kato of the Institute for Molecular Science, National Institutes of Natural Sciences developed a methodology for quantitatively describing the dynamic behaviors of complicated sugar chains in solution at atomic resolution by combining a sophisticated NMR spectroscopic approach with an ingenious molecular dynamics simulation technique. This study has just been published in Angewandte Chemie International Edition (published online on September 4, 2014), a scientific journal that is published on behalf of the German Chemical Society.

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