Phenotypic fluctuation rendered by a single genotype and evolutionary rate

Proteins are ideal systems to experimentally study stochastic complexity. They share many properties with supercooled liquids and glasses, but are functionally organized, perform biological work, and interact strongly with their surroundings. We describe the complexity of proteins, expressed through their hierarchically organized energy landscape, and characterize how fluctuations in the hydration shell and the bulk environment influence protein motions and functions.