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© Research
Publication : Proteins

Kinetic characterization of early intermediates in the folding of E. coli tryptophan-synthase beta 2 subunit

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Proteins - 01 Nov 1986

Blond S, Goldberg ME

Link to Pubmed [PMID] – 3329730

Proteins 1986 Nov;1(3):247-55

This report describes the use of fluorescence energy transfer between an intrinsic energy donor (tryptophan 177) and two chemically added acceptors to study intermediates in the folding of the beta 2 subunit of E. coli tryptophan-synthase. Two early folding steps are thus identified and characterized. One is very rapid (its rate constant at 12 degrees C is 0.02 sec-1) and corresponds to the folding of the N-terminal domain into a structure whose overall features approximate well those of the native domain. The second step is somewhat slower (its rate constant at 12 degrees C is 0.008 sec-1) and involves a conformational rearrangement of the N-terminal domain brought about by the interactions between the N- and C-terminal domains within a monomeric beta chain. This brings to five the number of intermediates which have been identified and ordered on the folding pathway of the dimeric beta 2 subunit.

https://www.ncbi.nlm.nih.gov/pubmed/3329730