Figure 3
From: Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini

Thermostability of OvTIM and variants and comparative analysis. (a) Thermal stability of wild-type and variants (AAA, ∆SAD, N115A, and N115A_∆SAD). (b) Melting temperature of variants based on the CD absorbance at 222 nm. (c) Superimposition of wild-type, AAA, and ∆SAD variant structures. N115 residues from wild-type, AAA, and ∆SAD are represented as a stick model. The disordered region of ∆SAD variant is represented as a dash. (b) Superimposition of the OvTIM, HsTIM, and ∆SAD_N115A structures.