Salt-Specific Suppression of the Cold Denaturation of Thermophilic Multidomain Initiation Factor 2.

ABSTRACT: Thermophilic proteins and enzymes are attractive for use in industrial applications due to their resistance against heat and denaturants. Here, we report on a thermophilic protein that is stable at high temperatures (T_{trs, hot} 67 °C) but undergoes significant unfolding at room temperature due to cold denaturation. Little is known about the cold denaturation of thermophilic proteins, although it can significantly limit their applications. We investigated the cold denaturation of thermophilic multidomain protein translation initiation factor 2 (IF2) from Thermus thermophilus. IF2 is a GTPase that binds to ribosomal subunits and initiator fMet-tRNA^fMet during the initiation of protein biosynthesis. In the presence of 9 M urea, measurements in the far-UV reg

SUBMITTER: Dzupponova V 

PROVIDER: S-EPMC10094840 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature