Two‐stage thermal unfolding of [Cys55]‐substituted Cro repressor of bacteriophage λ
- 9 September 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 289 (2) , 201-204
- https://doi.org/10.1016/0014-5793(91)81069-k
Abstract
It has been shown by scanning calorimetry and 1H NMR spectroscopy that thermal denaturation of mutant λ 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°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.Keywords
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