Protein stability and dynamics
Water mediates the interactions that govern the structural stability and functional dynamics of proteins. We study hydrophobic effects, cold denaturation, effects of osmolytes and denaturants, and the dynamical coupling between protein and water motions, including water-coupled intermittent (gating) dynamics in proteins.
Legend: Protein cold denaturation as seen from the solvent. Water 17O apparent dynamic perturbation factor (ADPF) versus temperature for ubiquitin (left) and apomyoglobin (right), showing the contributions from internal water (red) and surface hydration water in the native (blue) and cold-denatured (yellow) states. Apomyoglobin cold-denatures at –16 °C (midpoint), but ubiquitin does not cold-denature above –30 °C.
M Davidovic, C Mattea, J Qvist & B Halle, JACS 131, 1025–1036 (2009).
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