TY - JOUR
T1 - Flexibility damps macromolecular crowding effects on protein folding dynamics
T2 - Application to the murine prion protein (121-231)
AU - Bergasa-Caceres, Fernando
AU - Rabitz, Herschel A.
PY - 2014/1/20
Y1 - 2014/1/20
N2 - A model of protein folding kinetics is applied to study the combined effects of protein flexibility and macromolecular crowding on protein folding rate and stability. It is found that the increase in stability and folding rate promoted by macromolecular crowding is damped for proteins with highly flexible native structures. The model is applied to the folding dynamics of the murine prion protein (121-231). It is found that the high flexibility of the native isoform of the murine prion protein (121-231) reduces the effects of macromolecular crowding on its folding dynamics. The relevance of these findings for the pathogenic mechanism are discussed.
AB - A model of protein folding kinetics is applied to study the combined effects of protein flexibility and macromolecular crowding on protein folding rate and stability. It is found that the increase in stability and folding rate promoted by macromolecular crowding is damped for proteins with highly flexible native structures. The model is applied to the folding dynamics of the murine prion protein (121-231). It is found that the high flexibility of the native isoform of the murine prion protein (121-231) reduces the effects of macromolecular crowding on its folding dynamics. The relevance of these findings for the pathogenic mechanism are discussed.
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U2 - 10.1016/j.cplett.2013.11.035
DO - 10.1016/j.cplett.2013.11.035
M3 - Article
AN - SCOPUS:84890100996
SN - 0009-2614
VL - 591
SP - 207
EP - 211
JO - Chemical Physics Letters
JF - Chemical Physics Letters
ER -