PMID:10811909

Citation	Heidary, DK, O'Neill, JC Jr, Roy, M and Jennings, PA (2000) An essential intermediate in the folding of dihydrofolate reductase. Proc. Natl. Acad. Sci. U.S.A. 97:5866-70
Abstract	The folding of Escherichia coli dihydrofolate reductase was examined at pH 7.8 and 15 degrees C by using stopped-flow fluorescence and absorbance spectroscopies. The formation of a highly fluorescent intermediate occurs with relaxation times ranging between 142 and 343 msec, whereas stopped-flow absorbance spectroscopy using methotrexate binding assays shows a distinct lag phase during these time frames for the native state. The lag in absorbance kinetics and the lack of fast-track folding events indicate that the formation of this ensemble of intermediates is an obligatory step in the folding reaction.
Links	PubMed PMC18525 Online version:10.1073/pnas.100547697
Keywords	Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Escherichia coli/enzymology; Methotrexate/metabolism; Models, Molecular; Protein Binding; Protein Conformation; Protein Folding; Spectrometry, Fluorescence; Tetrahydrofolate Dehydrogenase/chemistry; Tetrahydrofolate Dehydrogenase/metabolism
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.