Differential scanning calorimetry demonstrates that the tryptophan repressor of Escherichia coli is unusually resistant to thermal denaturation. The dimeric protein undergoes reversible dissociative unfolding at pH 7.5 centered at about 90 degrees C. The thermal stability may be due in part to the unusual structure of the protein, which is composed of two identical intertwined polypeptide chains. Study holds ProTherm entries: 3001 Extra Details: tryptophan repressor; thermal stability; dimeric protein;,reversible dissociative unfolding
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:20 p.m.
|Number of data points||4|
|Proteins||Trp operon repressor ; Trp operon repressor|
|Assays/Quantities/Protocols||Experimental Assay: dCp ; Experimental Assay: dHcal ; Experimental Assay: Tm ; Experimental Assay: dHvH|
|Libraries||Mutations for sequence AQQSPYSAAMAEQRHQEWLRFVDLLKNAYQNDLHLPLLNLMLTPDEREALGTRVRIVEELLRGEMSQRELKNELGAGIATITRGSNSLKAAPVELRQWLEEVLLKSD|