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Based on these observations it was concluded that folding of permuted dihydrofolate reductase variants was terminated at the stage of the molten globule formation, whereas their interaction with ligands promoted structural adjustments and formation of active protein molecules, indicating ligand-induced transition from the molten globule to the native state (Uversky et al., 1996)

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Scholz RW, Graham KS, Gumpricht E, Reddy CC

Using density functional theory calculations, the catalytic cycle of the transformation of GSH to GSSG using Ru(II)-OH as a catalyst was calculated (Supplementary Tables 36)

PMID 28848356 Hubinger, J

In these simulations, the charge of K251 has a very large impact on interactions with the nucleotide: neutral K251 does not form substantial interactions, whereas positively (+1) charged K251 constantly binds to the -phosphate of ATP