Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Thermodynamics of the folding of D-glyceraldehyde-3-phosphate dehydrogenase assisted by protein disulfide isomerase studied by microcalorimetry.

Liang Y, Li J, Chen J, Wang CC

Thermodynamics of the refolding of denatured D-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) assisted by protein disulfide isomerase (PDI), a molecular chaperone, has been studied by isothermal microcalorimetry at different molar ratios of PDI/GAPDH and temperatures using two thermodynamic models proposed for chaperone-substrate binding and chaperone-assisted substrate folding, respectively. The binding of GAPDH folding intermediates to PDI is driven by a large favorable ... [more]

Eur. J. Biochem. Aug. 01, 2001; 268(15);4183-9 [Pubmed: 11488911]

Throughput

  • Low Throughput

Curated By

  • BioGRID