Proteins share important properties with glasses and supercooled liquids. They can assume a very large number of conformations (substates), show a glass transition, and exhibit alpha and beta fluctuations. In two respects, however, they differ. Proteins are designed for functions, glasses are not. External influences are crucial for proteins, for glasses they are less important. Proteins are surrounded by a hydration shell and embedded in a bulk solvent. The beta fluctuations in the hydration shell influence internal protein motions, the alpha fluctuations in the bulk affect the protein shape.         Four different transitions dominated the protein dynamics literature, the protein glass transition (PGT), the protein dynamic transition (PDT), the fragile-to-strong crossover (FSC), and the alpha-to-beta crossover. Using what is known from experiment about the effect of the hydration shell and the bulk solvent, and about the techniques used, the four transitions can either be explained or shown to be non-existent.

Glassy dynamics of proteins

244th National Meeting (2012)

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