In-situ measurement of 3-D protein structure inside living eukaryotic cells | 3/5/2009 | Staff
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Researchers from Tokyo Metropolitan University have successfully determined the high-resolution, three-dimensional structure of proteins inside living eukaryotic cells. They combined "in-cell" nuclear magnetic resonance (NMR) spectroscopy, a bioreactor system and cutting-edge computational algorithms to determine protein structures in crowded intracellular environments for the first time. The technique promises insight into the intracellular behavior of disease-causing proteins and novel drug screening applications, allowing in-situ visualization of how proteins respond to biochemical stimuli.

Eukaryotic cells are the building blocks of a vast range of organisms, including all fungi, plants and animals. Their internal structure is extremely complex and varied, with an intricate structural hierarchy and a vast range of biomacromolecules distributed around a cytoskeletal network. This has made it difficult to see what each protein inside the cells does in its natural environment, despite the obvious biomedical benefits of knowing, e.g. how a particular protein reacts when cells are subjected to chemical stimuli, like pharmaceutical drugs.

Challenge - Team - Tokyo - Metropolitan - University

To tackle this challenge, a team from Tokyo Metropolitan University led by Assistant Professor Teppei Ikeya and Professor Yutaka Ito applied nuclear magnetic resonance (NMR) spectroscopy measurements to specific proteins expressed inside sf9 cultured insect cells, a strain of cells originally derived from a type of moth larva widely used for protein production. The team's pioneering NMR work had already succeeded in elucidating high-resolution protein structures inside bacteria (non-eukaryotes). The problem with simply applying the same techniques to proteins in sf9 cells was the significantly lower concentration of target proteins and short lifetime...
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