NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics
Fig 4
Conformations of the refolded NS3pro in complex with NS2B (1–130) in the LMPC micelle.
(A) Far-UV CD spectra of the isolated NS3pro (black), NS2B (1–130) reconstituted in the LMPC micelle, refolded NS2B (48–100)-NS3pro complex at a molar ratio of 1:1 in the buffer at pH 7.5 (red), and refolded NS2B (1–130)-NS3pro complex reconstituted in the LMPC micelle in the buffer at pH 7.5 (blue). (B) HSQC spectrum of the full-length NS2B (1–130) reconstituted in the LMPC micelle in the buffer at pH 7.5. (C) HSQC spectra of the NS2B (48–130)-NS3pro complex in buffer (pH 7.5) (blue) and refolded NS2B (1–130)-NS3pro complex reconstituted in the LMPC micelle in the buffer at pH 7.5 (red). The green arrows are used to indicate the HSQC peaks of the refolded NS2B (1–130)-NS3pro complex which are not superimposable with those of the NS2B (48–130)-NS3pro complex.