TY - JOUR
T1 - A simple quantitative model of macromolecular crowding effects on protein folding
T2 - Application to the murine prion protein(121-231)
AU - Bergasa-Caceres, Fernando
AU - Rabitz, Herschel A.
PY - 2013/6/14
Y1 - 2013/6/14
N2 - A model of protein folding kinetics is applied to study the effects of macromolecular crowding on protein folding rate and stability. Macromolecular crowding is found to promote a decrease of the entropic cost of folding of proteins that produces an increase of both the stability and the folding rate. The acceleration of the folding rate due to macromolecular crowding is shown to be a topology-dependent effect. The model is applied to the folding dynamics of the murine prion protein (121-231). The differential effect of macromolecular crowding as a function of protein topology suffices to make non-native configurations relatively more accessible.
AB - A model of protein folding kinetics is applied to study the effects of macromolecular crowding on protein folding rate and stability. Macromolecular crowding is found to promote a decrease of the entropic cost of folding of proteins that produces an increase of both the stability and the folding rate. The acceleration of the folding rate due to macromolecular crowding is shown to be a topology-dependent effect. The model is applied to the folding dynamics of the murine prion protein (121-231). The differential effect of macromolecular crowding as a function of protein topology suffices to make non-native configurations relatively more accessible.
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U2 - 10.1016/j.cplett.2013.04.056
DO - 10.1016/j.cplett.2013.04.056
M3 - Article
AN - SCOPUS:84878595500
SN - 0009-2614
VL - 574
SP - 112
EP - 115
JO - Chemical Physics Letters
JF - Chemical Physics Letters
ER -