Conformational Entropy of Intrinsically Disordered Protein
- Authors
- Chong, Song-Ho; Ham, Sihyun
- Issue Date
- May-2013
- Publisher
- AMER CHEMICAL SOC
- Citation
- JOURNAL OF PHYSICAL CHEMISTRY B, v.117, no.18, pp 5503 - 5509
- Pages
- 7
- Journal Title
- JOURNAL OF PHYSICAL CHEMISTRY B
- Volume
- 117
- Number
- 18
- Start Page
- 5503
- End Page
- 5509
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/11280
- DOI
- 10.1021/jp401049h
- ISSN
- 1520-6106
- Abstract
- Intrinsically disordered proteins (IDPs), though lacking stable tertiary structures, are known to possess a certain amount of residual structure. Conformational disorder plays a crucial role through the conformational entropy in regulating protein-protein and protein ligand interactions involved in signaling and regulation, and also modulates protein aggregation and amyloidogenesis associated with a number of human diseases. However, a direct and quantitative connection between the residual structure and the conformational entropy remains to be established. Here we show using a novel computational approach that the conformational entropy of amyloid-beta protein, an IDP whose aggregation is associated with Alzheimer's disease, is significantly correlated with the contents of the residual helical structure, beta-sheet structure, and salt-bridge network. Identification of the thermodynamically significant residual structure is of fundamental importance for a comprehensive understanding of the relationship between the functional conformational disorder and the protein activity regulation, and will also serve the thermodynamic basis of the amyloid polymorphism.
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