Living cells contain high concentrations of macromolecules such as proteins, resulting in a crowded environment. The crowded environment significantly affects the state of hydration water around proteins. For isolated proteins, using molecular dynamics simulations, we study the transition between two distinct states of hydration water, states with small, disconnected clusters and states with a spanning hydrogen-bonded water network. With increasing hydration shell water molecules, a spanning H-bonded network was formed around protein surfaces via a percolation transition. We consider the nature of the surface water network for the ubiquitin system. We attempt to connect the protein-protein dimerization interface with the dynamical characteristics of the enveloping hydration layer of water molecules. We will provide further analysis of interactions of ubiquitin with binding motifs in model crowded cellular environments. We will also consider other protein systems such as hydrophobins and lysozyme.

Molecular dynamics study of spanning networks of protein hydration water

245th National Meeting (2013)

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