| 概 要 |
Cosolvents, sometimes also called osmolytes, bias protein folding equilibria towards the folded (stabilizers) or unfolded state (denaturants). In nature, this is exploited to control the stability of proteins and thus to counteract external perturbations like hydrostatic pressure. Abundantly found are the stabilizer trimethylamine-N-oxide (TMAO) and the denaturant urea.
In this talk, we will present molecular simulations of cosolute effects on aqueous protein and poeptide solutions. We will discuss how simulations give a detailed insight into the thermodynamic action of cosolutes, the underlying energetics, and the variety of binding geometries for typical peptide secondary structures. We will further use the molecular dynamics results for the improvement of heuristic models for cosolute effects, which are frequently employed for the analysis of experimental protein stability data. We will also address the interplay of cosolute effects and pressure effects.
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