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Stability of Proteins in aqueous solutions
The correct structure of protein in water is essential for all life on earth. The thermodynamics of protein folding depends critically on the solution composition. Some molecules like urea act denaturing, while molecules like trimethlyamine N-oxide stabilize the folded structure. We study the stability of peptides in solutions of urea, TMAO, salts etc. by molecular simulations. Thermodynamic properties are derived from a thorough statistical mechanical analysis of the results.
We use molecular dynamics simulations to study the properties of water at different hydrophobic surfaces like hydrogen-terminated diamond or alkane SAMs. Structural and dynamic properties are obtained.
A polyglycine chain
interacting with urea.
Publications:
Horinek, D.; Netz, R. R.
Can simulations quantitatively predict peptide transfer free energies to urea solutions? Thermodynamic concepts and force field limitations.
J. Phys. Chem. A 2011, 115, 6125
N. Schwierz, D. Horinek, R. R. Netz
Ion specificity as a function of surface charge and polarity: direct, reversed, and partially reversed Hofmeister series.
Langmuir, 2010, 26, 7370
