title: Foldable subunits of helix protein.
abstract: Detection of foldable subunits in proteins is an important approach to understand their evolutions and find building motifs for de novo protein design. Using united-residue model, we simulated the folding of a six-helix protein with a length of 120 amino acids (C-terminal domain of Ku86). The folding behaviors, structural topology and sequence repetition of this protein all suggest that it may have a two-fold quasi-repetition or symmetry in its sequence and structure. Therefore, we simulated the folding of its two halves (1-60 and 61-120 amino acids) and find that they can fold into native conformations independently. It is also found that their folding behaviors are very similar to other three-helix bundles. This suggests that this protein may be divided into two foldable halves.
authors.affiliation: Biomolecular Physics and Modeling Group, Department of Physics, Huazhong University of Science and Technology, Wuhan 430074, China.
authors.forename: Yi
authors.initials: Y
authors.lastname: He
authors.forename: Rui
authors.initials: R
authors.lastname: Zhou
authors.forename: Yanzhao
authors.initials: Y
authors.lastname: Huang
authors.forename: Yi
authors.initials: Y
authors.lastname: Xiao
mesh_terms: D000818:Animals; D034961:Antigens, Nuclear / Q000737:chemistry / Q000502:physiology*; D003198:Computer Simulation; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000502:physiology*; D000072200:Ku Autoantigen; D008958:Models, Molecular; D017510:Protein Folding; D021122:Protein Subunits / Q000737:chemistry / Q000502:physiology*
chemical_list: D034961:Antigens, Nuclear; D004268:DNA-Binding Proteins; D021122:Protein Subunits; D000072200:Ku Autoantigen