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.

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