期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 524, 期 2, 页码 123-131出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2012.04.024
关键词
Conformational ensemble; Coupled binding and folding; Signaling and regulation
资金
- National Science Foundation [MCB 0952514]
- Johnson Center for Basic Cancer Research of Kansas State University
- Division Of Computer and Network Systems
- Direct For Computer & Info Scie & Enginr [1126709] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0952514] Funding Source: National Science Foundation
Intrinsically disordered proteins (IDPs) are an important class of functional proteins that is highly prevalent in biology and has broad association with human diseases. In contrast to structured proteins, free IDPs exist as heterogeneous and dynamical conformational ensembles under physiological conditions. Many concepts have been discussed on how such intrinsic disorder may provide crucial functional advantages, particularly in cellular signaling and regulation. Establishing the physical basis of these proposed phenomena requires not only detailed characterization of the disordered conformational ensembles, but also mechanistic understanding of the roles of various ensemble properties in IDP interaction and regulation. Here, we review the experimental and computational approaches that may be integrated to address many important challenges of establishing a structural basis of IDP function, and discuss some of the key emerging ideas on how the conformational ensembles of IDPs may mediate function, especially in coupled binding and folding interactions. (C) 2012 Elsevier Inc. All rights reserved.
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