It has been shown by scanning calorimetry and 1H NMR spectroscopy that thermal denaturation of mutant lambda phage cro repressor in which Val55 was substituted for Cys, proceeds in 2 stages in contrast to the wild type protein. At neutral pH values, an additional cooperative transition has been observed at about 100 degrees C. Calorimetric measurements on the mutant and its tryptic fragment lead to the conclusion that the two-stage character of thermal unfolding of the mutant is due to a disruption of an additional cooperative domain in the dimer molecule which is stabilized by the S-S crosslink. Study holds ProTherm entries: 10812, 10813, 10814 Extra Details: cro repressor; mutant; thermal denaturation; S-S bond;,scanning calorimetry; 1H NMR
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:41 p.m.
|Number of data points||6|
|Proteins||Regulatory protein cro ; Regulatory protein cro|
|Assays/Quantities/Protocols||Experimental Assay: dHcal ; Experimental Assay: Tm|
|Libraries||Mutations for sequence MEQRITLKDYAMRFGQTKTAKDLGVYQSAINKAIHAGRKIFLTINADGSVYAEEVKDGEVKPFPSNKKTTA|