Abstract
We investigate the thermodynamics of hydrophobic oligomer collapse using a water-explicit, three-dimensional lattice model. The model captures several aspects of protein thermodynamics, including the emergence of cold- and thermal-unfolding, as well as unfolding at high solvent density (a phenomenon akin to pressure-induced denaturation). We show that over a range of conditions spanning a ≈14% increase in solvent density, the oligomer transforms into a compact, strongly water-penetrated conformation at low temperature. This contrasts with thermal unfolding at high temperature, where the system "denatures" into an extended random coil conformation. We report a phase diagram for hydrophobic collapse that correctly captures qualitative aspects of cold and thermal unfolding at low to intermediate solvent densities.
Original language | English (US) |
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Pages (from-to) | 9540-9548 |
Number of pages | 9 |
Journal | Journal of Physical Chemistry B |
Volume | 116 |
Issue number | 31 |
DOIs | |
State | Published - Aug 9 2012 |
All Science Journal Classification (ASJC) codes
- Physical and Theoretical Chemistry
- Surfaces, Coatings and Films
- Materials Chemistry