Abstract
Abstract
The human proteome is enriched in proteins that do not fold into a stable 3D structure. These intrinsically disordered proteins (IDPs) spontaneously fluctuate between a large number of configurations in their native form. Remarkably, the disorder does not lead to dysfunction as with denatured folded proteins. In fact, unlike denatured proteins, recent evidence strongly suggests that multiple biological functions stem from such structural plasticity. Here, focusing on the nanometer length-scale, we review the latest advances in IDP research and discuss some of the future directions in this highly promising field.
Funder
National Science Foundation
Israel Science Foundation
United States-Israel Binational Science Foundation
Subject
Electrical and Electronic Engineering,General Materials Science,Biomedical Engineering,Atomic and Molecular Physics, and Optics,General Chemistry,Bioengineering
Cited by
7 articles.
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