Balance between hydration enthalpy and entropy is important for ice binding surfaces in Antifreeze Proteins.

ABSTRACT: Antifreeze Proteins (AFPs) inhibit the growth of an ice crystal by binding to it. The detailed binding mechanism is, however, still not fully understood. We investigated three AFPs using Molecular Dynamics simulations in combination with Grid Inhomogeneous Solvation Theory, exploring their hydration thermodynamics. The observed enthalpic and entropic differences between the ice-binding sites and the inactive surface reveal key properties essential for proteins in order to bind ice: While entropic contributions are similar for all sites, the enthalpic gain for all ice-binding sites is lower than for the rest of the protein surface. In contrast to most of the recently published studies, our analyses show that enthalpic interactions are as important as an ice-like pre-ordering. Based on these

SUBMITTER: Schauperl M 

PROVIDER: S-EPMC5605524 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature