Fig. 1: Metamorphic proteins undergo large-scale conformational rearrangements. | Communications Chemistry

Fig. 1: Metamorphic proteins undergo large-scale conformational rearrangements.

From: Crowded environments tune the fold-switching in metamorphic proteins

Fig. 1

a The interconversion between inactive ground-state KaiB (gsKaiB, PDB:2QKE) and active fold-switched KaiB (fsKaiB, PDB:5JYT). b The interconversion between inactive Ltn10-like XCL1 (PDB:1J8I) adopts α + β fold and active Ltn40-like XCL1 (PDB:2JP1) adopts all-β-sheet fold. The gray segments have no changes in secondary structure in both thermodynamically accessible states and the same color represents same primary structure but adopts distinct secondary structures in both states. k1 and k-1 correspond to the forward interconversion from inactive form (gsKaiB and Ltn10-like XCL1) to active form (fsKaiB and Ltn40-like XCL1) and the reverse interconversion from active form to inactive form, respectively.

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