Water can act as a conformational lubricant for protein folding. The giant muscle protein titin is a roughly 30,000 amino acid long filament which plays a number of important roles in contraction and elasticity. For example, upon stretching in muscle some of titin's protein domains can unfold one-by-one permitting titin to retain elastic properties in muscle over a very wide range of length. To examine in atomic detail the dynamics and structure-function relationships of this behavior, SMD simulations of force-induced titin domain unfolding were performed in close collaboration with atomic force microscopy observations. The simulations led to the discovery that water molecules play an essential role in breaking sets of hydrogen bonds that control the unfolding of titin's domains (see resulting publication).