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Determination of protein structures using NMR chemical shifts

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Chemical shifts are the most readily and accurately measurable NMR parameters and they reflect with great specificity the conformations of both native and non-native states of proteins. I will describe a procedure through which chemical shifts can be used to determine the structures of proteins at high resolution and without the need for additional experimental information. The approach involves the use of chemical shifts to guide the assembly of the protein conformation from structural fragments and its refinement through restrained simulations. This strategy should have a very significant impact on the extension of the use of NMR spectroscopy for larger and more complex problems than currently believed to be feasible.

This talk is part of the Theory of Condensed Matter series.

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