Literature summary for 1.5.1.3 extracted from

Arai, M.; Kondrashkina, E.; Kayatekin, C.; Matthews, C.R.; Iwakura, M.; Bilsel, O.
Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate reductase, an alpha/beta-type protein (2007), J. Mol. Biol., 368, 219-229.

Crystallization (Commentary)

Crystallization (Comment)	Organism
microsecond compaction dynamics study of the folding. A significant collapse of the radius of gyration from 30 A to 23.2 A occurs within 0.3 sec after the initiatiation of refolding by a urea dilution jump. the subsequent folding occurs on a considerably longer time scale. Experimental data may best be explained by the specific hydrophobic collapse model. The folding trajectory of the protein is located between those of alpha-helical and beta-sheet proteins	Escherichia coli

Crystallization (Comment)

Organism

microsecond compaction dynamics study of the folding. A significant collapse of the radius of gyration from 30 A to 23.2 A occurs within 0.3 sec after the initiatiation of refolding by a urea dilution jump. the subsequent folding occurs on a considerably longer time scale. Experimental data may best be explained by the specific hydrophobic collapse model. The folding trajectory of the protein is located between those of alpha-helical and beta-sheet proteins

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ABQ4	-	-

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Release 2023.1 (January 2023)