Gaussian model of protein folding

The thermodynamics and kinetics of protein folding depend on the sequence o f monomer units along the chain. To explore the sequence dependence, curren t modeling-all-atom simulations and lattice models, for example-require tim e-consuming computer simulations. There are currently no analytical models by which folding properties can be computed directly from the monomer seque nce. Here we introduce a simple analytical model of folding, based on assum ing springlike forces for covalent and noncovalent interactions. Thermodyna mic and kinetic properties of folding can be obtained directly for specific sequences in Go-like models. Remarkably, although it is a continuum model, some choices of parameters give the same stable conformations as in the co rresponding lattice model. The main point of elasticity-based folding model s is that their properties can be understood in complete detail, and with l ittle computational investment. This may be useful for understanding how th e shapes of energy landscapes, including stable states and kinetic barriers , depend on amino acid sequence. (C) 2000 American Institute of Physics. [S 0021-9606(00)51101-5].