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Intro to Protein Folding. Ken Dill Many of the elementary principles of protein folding are being explored in simple physical models. These models aim to capture some of the essential forces -- (i) that nonpolar monomers avoid water, (ii) that chain molecules have internal degrees of freedom, and (iii) that protein conformations are severely limited by steric constraints. Even without including atomic detail, such models, explored by statistical mechanical methods, reproduce many aspects of protein folding behavior, including collapse cooperativity, hydrophobic cores, secondary structures, tertiary symmetries, and folding kinetics that can include single exponentials or more complex behavior. Such models lead to the language of energy landscapes and folding funnels for describing the thermodynamics and kinetics. These models are also useful for exploring ligand binding properties, including some interesting and unexpected behaviors. Such modelling has been suggesting ways to develop better energy functions, better ways to treat conformational entropies in polymers, and faster conformational search strategies for computer prediction algorithms. ## Back to the list of abstracts