Please use this identifier to cite or link to this item:
|Title:||Accessibility of compact structures and prion-like protein folding property|
|Authors:||Chen, H. |
Monte Carlo simulation
|Citation:||Chen, H., Chan, G.K., Chih, Y.L., Zhou, X. (2005-11-10). Accessibility of compact structures and prion-like protein folding property. Modern Physics Letters B 19 (25) : 1241-1252. ScholarBank@NUS Repository. https://doi.org/10.1142/S0217984905009183|
|Abstract:||Based on two-dimensional Gō model of proteins and Monte Carlo simulation method, it is found that different compact conformations have different accessibility, i.e., some are easy to reach in the Monte Carlo simulation from a random conformation, while others are not. The logarithm of folding time is approximately a linear function of the contact order of the native conformation, which is consistent with published experimental results. Transition barrier is the main factor to determine the folding time at low temperature when proteins are stable. To fold to native structure with bigger contact order, higher barrier needs to be overcome. To study the folding properties of some prion-like proteins which have two possible conformations, the normal Gō model is extended to double-Gō model with two native states. In folding simulations, the native state with high accessibility is reached with much higher probability than the other. The accessibility of compact structures determines which structure is easy to reach in folding process. © World Scientific Publishing Company.|
|Source Title:||Modern Physics Letters B|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jun 8, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.