期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 74, 期 17, 页码 3185-3204出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-017-2561-6
关键词
Intrinsic disorder; In cell NMR; Intracellular protein delivery; Conformational ensemble
资金
- Research Foundation Flanders (FWO) [G.0029.12]
- FWO
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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