Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 74, Issue 17, Pages 3185-3204Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-017-2561-6
Keywords
Intrinsic disorder; In cell NMR; Intracellular protein delivery; Conformational ensemble
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Funding
- Research Foundation Flanders (FWO) [G.0029.12]
- FWO
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There is ample evidence that many proteins or regions of proteins lack a well-defined folded structure under native-like conditions. These are called intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs). Whether this intrinsic disorder is also their main structural characteristic in living cells has been a matter of intense debate. The structural analysis of IDPs became an important challenge also because of their involvement in a plethora of human diseases, which made IDPs attractive targets for therapeutic development. Therefore, biophysical approaches are increasingly being employed to probe the structural and dynamical state of proteins, not only in isolation in a test tube, but also in a complex biological environment and even within intact cells. Here, we survey direct and indirect evidence that structural disorder is in fact the physiological state of many proteins in the proteome. The paradigmatic case of alpha-synuclein is used to illustrate the controversial nature of this topic.
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