Parts | Days | Selection | Search | Downloads | Help

BP: Fachverband Biologische Physik

BP 25: Protein Structure and Folding

BP 25.5: Talk

Thursday, February 28, 2008, 15:30–15:45, PC 203

Insights from atomistic computer simulations of halophilic proteins — •Joachim Dzubiella — Physics Department, Technical University Munich, Germany

Halophilic (salt-loving) proteins, typically found in Archaea, can maintain their native structure and function in aqueous environment only at relatively high salt concentrations (>1-2M). As they are highly negatively charged at physiological conditions the competition between hydrophobic and hydrophilic solvation is strongly amplified and tuned by salt type and concentration. By performing atomistic molecular dynamics (MD) computer simulations the influence of salt on effective interactions between amino acids, protein secondary structures, and the stability of small coiled-coil proteins is investigated. Possible salt-induced specific and non-specific (de)stabilization mechanisms are identified and critically discussed.

100% | Screen Layout | Deutsche Version | Contact/Imprint/Privacy
DPG-Physik > DPG-Verhandlungen > 2008 > Berlin