Average conformations determined from PRE data provide high-resolution maps of transient tertiary interactions in disordered proteins.

Abstract

In the last decade it has become evident that disordered states of proteins play important physiological and pathological roles and that the transient tertiary interactions often present in these systems can play a role in their biological activity. The structural characterization of such states has so far largely relied on ensemble representations, which… (More)
DOI: 10.1016/j.bpj.2013.02.019

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Cite this paper

@article{SilvestreRyan2013AverageCD, title={Average conformations determined from PRE data provide high-resolution maps of transient tertiary interactions in disordered proteins.}, author={Jordi Silvestre-Ryan and Carlos W. Bertoncini and Robert Bryn Fenwick and Santiago Esteban-Mart{\'i}n and Xavier Salvatella}, journal={Biophysical journal}, year={2013}, volume={104 8}, pages={1740-51} }