Two-stage thermal unfolding of [Cys55]-substituted Cro repressor of bacteriophage lambda.


Abstract

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

Submission Details

ID: kFhG5QLP4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:41 p.m.

Version: 1

Publication Details
Gitelson GI;Griko Yu V;Kurochkin AV;Rogov VV;Kutyshenko VP;Kirpichnikov MP;Privalov PL,FEBS Lett. (1991) Two-stage thermal unfolding of [Cys55]-substituted Cro repressor of bacteriophage lambda. PMID:1833238
Additional Information

Sequence Assay Result Units