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Research Seminar: Characterization of intrinsically disordered proteins and their dynamic complexes using NMR spectroscopy.

27 September 2017

Dr. Malene Ringkgøbing-Jensen, Institute of Structural Biology, Grenoble, France

Tuesday 3rd October, 1.00 p.m., Stacey Lecture Theatre 1

Over the last two decades, it has become increasingly clear that a large fraction (up to 40%) of the proteins encoded by the human genome are intrinsically disordered or contain disordered regions of significant length. These intrinsically disordered proteins (IDPs) play important regulatory roles throughout biology, and they have been intimately linked to a number of human diseases. Nuclear magnetic resonance (NMR) spectroscopy is uniquely suited for tackling such dynamic protein systems providing information about conformational propensities and interactions mechanisms at atomic resolution. In this presentation, examples will be given of the characterization of functional protein disorder using NMR spectroscopy in important biological systems such as viruses and the mitogen-activated protein kinase (MAPK) cell signaling pathways.


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School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ

Last Updated: 27/09/2013