Please use this identifier to cite or link to this item:
|Title:||Optimal atomic-resolution structures of prion AGAAAAGA amyloid fibrils|
|Keywords:||Hybrid computational algorithms|
Optimizing molecular structures
|Citation:||Zhang, J., Sun, J., Wu, C. (2011). Optimal atomic-resolution structures of prion AGAAAAGA amyloid fibrils. Journal of Theoretical Biology 279 (1) : 17-28. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jtbi.2011.02.012|
|Abstract:||X-ray crystallography is a powerful tool to determine the protein 3D structure. However, it is time-consuming and expensive, and not all proteins can be successfully crystallized, particularly for membrane proteins. Although nuclear magnetic resonance (NMR) spectroscopy is indeed a very powerful tool in determining the 3D structures of membrane proteins, it is also time-consuming and costly. To the best of the authors' knowledge, there is little structural data available on the AGAAAAGA palindrome in the hydrophobic region (113-120) of prion proteins due to the noncrystalline and insoluble nature of the amyloid fibril, although many experimental studies have shown that this region has amyloid fibril forming properties and plays an important role in prion diseases. In view of this, the present study is devoted to address this problem from computational approaches such as global energy optimization, simulated annealing, and structural bioinformatics. The optimal atomic-resolution structures of prion AGAAAAGA amyloid fibils reported in this paper have a value to the scientific community in its drive to find treatments for prion diseases. © 2011.|
|Source Title:||Journal of Theoretical Biology|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Dec 10, 2018
WEB OF SCIENCETM
checked on Nov 26, 2018
checked on Dec 8, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.