Article
Extreme temperature tolerance of a hyperthermophilic protein coupled to residual structure in the unfolded state.
Journal of molecular biology - 13 Jun 2008
Wallgren Marcus, Adén Jörgen, Pylypenko Olena, Mikaelsson Therese, Johansson Lennart B-A, Rak Alexey, Wolf-Watz Magnus
Abstract excerpt
Understanding the mechanisms that dictate protein stability is of large relevance, for instance, to enable design of temperature-tolerant enzymes with high enzymatic activity over a broad temperature interval. In an effort to identify such mechanisms, we have performed a detailed comparative study of the folding thermodynamics and kinetics of the ribosomal protein S16 isolated from a mesophilic (S16(meso)) and...
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