منابع مشابه
Simple model of protein folding kinetics.
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 equatio...
متن کاملA simple theory of protein folding kinetics
We present a simple model of protein folding dynamics that captures key qualitative elements recently seen in all-atom simulations. The goals of this theory are to serve as a simple formalism for gaining deeper insight into the physical properties seen in detailed simulations as well as to serve as a model to easily compare why these simulations suggest a different kinetic mechanism than previo...
متن کاملThe topomer search model: A simple, quantitative theory of two-state protein folding kinetics.
Most small, single-domain proteins fold with the uncomplicated, single-exponential kinetics expected for diffusion on a smooth energy landscape. Despite this energetic smoothness, the folding rates of these two-state proteins span a remarkable million-fold range. Here, we review the evidence in favor of a simple, mechanistic description, the topomer search model, which quantitatively accounts f...
متن کاملA simple model for calculating the kinetics of protein folding from three-dimensional structures.
An elementary statistical mechanical model was used to calculate the folding rates for 22 proteins from their known three-dimensional structures. In this model, residues come into contact only after all of the intervening chain is in the native conformation. An additional simplifying assumption is that native structure grows from localized regions that then fuse to form the complete native mole...
متن کاملProtein Folding: Simple Models
Doublié, S., Sawaya, M.R., and Ellenberger, T. (1999). Struct. Fold. son and Beese, 2004). The same mispair, on the other Des. 7, R31–R35. hand, is poorly extended by Dpo4: it was shown to form Echols, H., and Goodman, M.F. (1991). Annu. Rev. Biochem. 60, a reverse wobble, which misaligns the 3 -end of the 477–511. primer and therefore precludes nucleophilic attack (TrinHatahet, Z., Zhou, M., R...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1995
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.92.21.9801