FEBS Letters | |
Two‐stage thermal unfolding of [Cys55]‐substituted Cro repressor of bacteriophage λ | |
Kutyshenko, V.P.2  Gitelson, G.I.1  Privalov, P.L.1  Griko, Yu.V.1  Rogov, V.V.1  Kurochkin, A.V.3  Kirpichnikov, M.P.3  | |
[1] Institute of Protein Research, Academy of Sciences of the USSR, Pushchino, Moscow Region 142292, USSR;Institute of Biological Physics, Academy of Sciences of the USSR, Pushchino, Moscow Region 142292, USSR;V.A. Engelhardt Institute of Molecular Biology, Academy of Sciences of the USSR, Moscow 117984, USSR | |
关键词: Cro repressor; Mutant; Thermal denaturation; S–S bond; Scanning calorimetry; 1H NMR; | |
DOI : 10.1016/0014-5793(91)81069-K | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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