Linking folding and binding.

Abstract

Many cellular proteins are intrinsically disordered and undergo folding, in whole or in part, upon binding to their physiological targets. The past few years have seen an exponential increase in papers describing characterization of intrinsically disordered proteins, both free and bound to targets. Although NMR spectroscopy remains the favored tool, a number of new biophysical techniques are proving exceptionally useful in defining the limits of the conformational ensembles. Advances have been made in prediction of the recognition elements in disordered proteins, in elucidating the kinetics and mechanism of the coupled folding and binding process, and in understanding the role of post-translational modifications in tuning the biological response. Here we review these and other recent advances that are providing new insights into the conformational propensities and interactions of intrinsically disordered proteins and are beginning to reveal general principles underlying their biological functions.

DOI: 10.1016/j.sbi.2008.12.003

3 Figures and Tables

0100200300200920102011201220132014201520162017
Citations per Year

1,359 Citations

Semantic Scholar estimates that this publication has 1,359 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Wright2009LinkingFA, title={Linking folding and binding.}, author={Peter E. Wright and H Jane Dyson}, journal={Current opinion in structural biology}, year={2009}, volume={19 1}, pages={31-8} }