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Decoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding

Fig 1

DapA structure.

A) The protein is composed of eleven α-helices surrounding the β-barrel superstructure composed of eight parallel β-strands shown in red and blue, respectively. B) Schematic representation of DapA topology displaying (α/β)8 TIM barrel fold along with C-terminal α-helices (α9–11). The terminal residues of each secondary structural elements are labeled.

Fig 1