Thermodynamics and kinetics of downhill protein folding investigated with a simple statistical mechanical model

2002 ◽  
Vol 90 (4-5) ◽  
pp. 1522-1528 ◽  
Author(s):  
Victor Muñoz
Keyword(s):  
Protein Folding ◽  
Mechanical Model ◽  
Thermodynamics And Kinetics ◽  
Statistical Mechanical Model ◽  
Statistical Mechanical ◽  
Kinetics Of

scholarly journals Cooperativity and modularity in protein folding

2016 ◽  
Author(s):  
Masaki Sasai ◽  
George Chikenji ◽  
Tomoki P. Terada
Keyword(s):  
Protein Folding ◽  
Mechanical Model ◽  
Energy Landscape ◽  
Native Conformation ◽  
Folding Nucleus ◽  
Modern Methods ◽  
Complex Topology ◽  
Statistical Mechanical Model ◽  
Statistical Mechanical ◽  
Dynamical Features

AbstractA simple statistical mechanical model proposed by Wako and Saitô has explained the aspects of protein folding surprisingly well. This model was systematically applied to multiple proteins by Muñoz and Eaton and has since been referred to as the Wako-Saitô-Muñoz-Eaton (WSME) model. The success of the WSME model in explaining the folding of many proteins has verified the hypothesis that the folding is dominated by native interactions, which makes the energy landscape globally biased toward native conformation. Using the WSME and other related models, Saitô emphasized the importance of the hierarchical pathway in protein folding; folding starts with the creation of contiguous segments having a native-like configuration and proceeds as growth and coalescence of these segments. The ϕ-values calculated for barnase with the WSME model suggested that segments contributing to the folding nucleus are similar to the structural modules defined by the pattern of native atomic contacts. The WSME model was extended to explain folding of multi-domain proteins having a complex topology, which opened the way to comprehensively understanding the folding process of multi-domain proteins. The WSME model was also extended to describe allosteric transitions, indicating that the allosteric structural movement does not occur as a deterministic sequential change between two conformations but as a stochastic diffusive motion over the dynamically changing energy landscape. Statistical mechanical viewpoint on folding, as highlighted by the WSME model, has been renovated in the context of modern methods and ideas, and will continue to provide insights on equilibrium and dynamical features of proteins.

scholarly journals Downhill versus two-state protein folding in a statistical mechanical model

2007 ◽  
Vol 126 (21) ◽  
pp. 215103 ◽  
Author(s):  
Pierpaolo Bruscolini ◽  
Alessandro Pelizzola ◽  
Marco Zamparo
Keyword(s):  
Protein Folding ◽  
Mechanical Model ◽  
Statistical Mechanical Model ◽  
Statistical Mechanical
Sign in / Sign up

Export Citation Format

Share Document