title: Hidden symmetries in the primary sequences of beta-barrel family.
abstract: In this paper, we analyze the symmetries of beta-barrel proteins at both structure and sequence levels by using a modified recurrent quantification analysis. It shows that the structures and sequences have the same two-fold symmetry, although the later diverged considerably. This result may be helpful to understand the mechanism of protein evolution.
authors.affiliation: Biomolecular Physics and Modeling Group, Department of Physics, Huazhong University of Science and Technology, Wuhan 430074, Hubei, China.
authors.forename: Xiaofeng
authors.initials: X
authors.lastname: Ji
authors.forename: Hanlin
authors.initials: H
authors.lastname: Chen
authors.forename: Yi
authors.initials: Y
authors.lastname: Xiao
mesh_terms: D000595:Amino Acid Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins