Standard Conformations of β-Arches in β-Solenoid Proteins

摘要: Strand-turn-strand motifs found in β-helical (more generally, β-solenoid) proteins differ fundamentally from those globular proteins. The latter are primarily β-hairpins which the two strands form an antiparallel β-sheet. In former, relatively rotated by ∼90° around strand axes so that they interact via side-chains, not polypeptide backbones. We call structures, β-arches, and their turns, β-arcs. β-solenoid proteins, β-arches stack in-register to β-arcades parallel β-sheets assembled corresponding successive layers. number of β-solenoids whose three-dimensional structures have been determined is now large enough support a detailed analysis classification β-arc conformations. Here, we present systematic account β-arcs distinguished residues, conformations, propensity into arcades with other like or unlike arches. trends emerge this implications for sequence-based detection structural prediction as well identification amyloidogenic sequences elucidation amyloid fibril structures.