Literature summary for 1.5.1.3 extracted from

Horst, R.; Fenton, W.A.; Englander, S.W.; Wuethrich, K.; Horwich, A.L.
Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution (2007), Proc. Natl. Acad. Sci. USA, 104, 20788-20792.

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P00374	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
NMR measurements of amide proton exchange protection during folding in the presence of methotrextae and ATP either free in solution or inside the stable cavity formed between a single ring variant of GroEL, SR1, and GroES chaperonins. In the SR1-GroES-mediated reaction, recovery of dihydrofolate reductase is twofold higher than in the spontaneous reaction. In both reactions, folding follows the same trajectories	Homo sapiens

Renatured (Comment)

Organism

NMR measurements of amide proton exchange protection during folding in the presence of methotrextae and ATP either free in solution or inside the stable cavity formed between a single ring variant of GroEL, SR1, and GroES chaperonins. In the SR1-GroES-mediated reaction, recovery of dihydrofolate reductase is twofold higher than in the spontaneous reaction. In both reactions, folding follows the same trajectories

Homo sapiens

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Release 2023.1 (January 2023)