Literature summary for 1.5.1.3 extracted from

Svensson, A.K.; Zitzewitz, J.A.; Matthews, C.R.; Smith, V.F.
The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli (2006), Protein Eng. Des. Sel., 19, 175-185.

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Protein Variants

Protein Variants	Comment	Organism
additional information	permutations in the N- and C-terminal domain show that for equilibrium and kinetic folding mechanism, a continuous adenosine-binding domain is required for a stable thermal intermediate and a continuous discontinuous loop domain is required for a stable urea intermediate	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ABQ4	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	for equilibrium and kinetic folding mechanism, a continuous adenosine-binding domain is required for a stable thermal intermediate and a continuous discontinuous loop domain is required for a stable urea intermediate	Escherichia coli

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Release 2023.1 (January 2023)