Simple model of protein folding kinetics.

AUTOR(ES)

Zwanzig, R

RESUMO

A simple model of the kinetics of protein folding is presented. The reaction coordinate is the "correctness" of a configuration compared with the native state. The model has a gap in the energy spectrum, a large configurational entropy, a free energy barrier between folded and partially folded states, and a good thermodynamic folding transition. Folding kinetics is described by a master equation. The folding time is estimated by means of a local thermodynamic equilibrium assumption and then is calculated both numerically and analytically by solving the master equation. The folding time has a maximum near the folding transition temperature and can have a minimum at a lower temperature.

Documentos Relacionados

• Cooperativity in protein-folding kinetics.
• A simple model for calculating the kinetics of protein folding from three-dimensional structures
• A microscopic model of enzyme kinetics.
• The precursor of beta-lactamase: purification, properties and folding kinetics.
• Nonglassy kinetics in the folding of a simple single-domain protein