Before revision: This region belongs to the N-terminal unstructured region ( 1-123 ) of prion proteins , the structure of which has proved hard to determine using NMR spectroscopy or X-ray crystallography due to the insoluble and noncrystalline nature of the amyloid fibril . However, computer computational optimization can easily obtain a description of this peptide at a submicroscopic level. The hybrid methods presented in this paper will be applied to construct amyloid fibril molecular structures of the prion 113-120 region .
After revision: This region belongs to the N-terminal unstructured region ( 1-123 ) of prion proteins , the structure of which has proved hard to determine using NMR spectroscopy or X-ray crystallography due to the insoluble and noncrystalline nature of the amyloid fibril , little structural data on the AGAAAAGA is available. This paper introduces a simple optimization strategy approach to address the 3D atomic-resolution structure of prion AGAAAAGA amyloid fibrils. Atomic-resolution structures of prion AGAAAAGA amyloid fibrils got in this paper are useful for the drive to find treatments for prion diseases in the field of medicinal chemistry .