| Abstract
| - Molecular simulations, comprising models with atomic details ofpolypeptide and solvent as well as minimalist models employingonly Cα atoms, are being used with specialized simulation methodsfrom statistical mechanics to examine fundamental questions inpeptide and protein folding mechanism, kinetics, and thermodynamics. Detailed calculations of free energy changes along coordinates describing the formation of hydrogen-bonding interactionsin helical, turn, and β-sheet models provide insights into the timescale and mechanism of secondary structure formation. Potentialroles for these processes in directing protein folding are alsoelucidated by such calculations. Analogous methodologies extendedto more complex polypeptides with tertiary structures (proteins)are used to explore global questions about protein folding landscapes, to delineate atomic details of folding mechanism, and toelucidate putative roles for solvent in the late stages of folding.
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