Ontology highlight
ABSTRACT:
SUBMITTER: Li IT
PROVIDER: S-EPMC3189081 | biostudies-other | 2011 Oct
REPOSITORIES: biostudies-other
Li Isaac T S IT Walker Gilbert C GC
Proceedings of the National Academy of Sciences of the United States of America 20110912 40
Hydrophobicity underpins self-assembly in many natural and synthetic molecular and nanoscale systems. A signature of hydrophobicity is its temperature dependence. The first experimental evaluation of the temperature and size dependence of hydration free energy in a single hydrophobic polymer is reported, which tests key assumptions in models of hydrophobic interactions in protein folding. Herein, the hydration free energy required to extend three hydrophobic polymers with differently sized aroma ...[more]