The Dynamics of Protein Disorder and its Evolution

Gustavo Caetano-Anolles, University of Illinois at Urbana-Champaign

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Disordered proteins play crucial physiological roles in organisms. However, they pose an enormous experimental challenge due to the heterogeneous conformational ensemble they sample at very short time scales. In a molecular simulation study we will monitor distance fluctuations of a given pair of residues in a nucleoporin peptide of growing length. We will test if conformational movement of disordered segments match the slow dynamics revealed by single molecule Förster resonance energy transfer experiments. Results could challenge the paradigm of disordered proteins being extraordinarily dynamic and will provide proof-of-concept for an all-encompassing analysis of protein flexibility and disorder.