Before revision: To date , there is little structural data available on the AGAAAAGA palindrome in the hydrophobic region (113-120) of prion proteins  , although many experimental studies have shown that this region has amyloid fibril forming properties . This region belongs to the N-terminal unstructured region (1-123) of prions, the structure of which has proved hard to determine using NMR or X-ray crystallography. Computational optimization approaches , however, allow us to obtain a description of prion 113-120 peptide at a microscopic level. Zhang (J. Mol. Model., 2010, DOI: 10.1007/s00894-010-0691-y) using the traditional local optimization search steepest descent and conjugate gradient methods hybridized with the standard global optimization search simulated annealingmethod successfully constructed three atomic-resolution structures of prion AGAAAAGA amyloid fibrils.
After revision: To date , there is little structural data available on the AGAAAAGA palindrome in the hydrophobic region (113-120) of prion proteins , 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 fibrils.