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• W2044713411 abstract "An important question in protein folding is whether the folding mechanism is sequence dependent and conserved for homologous proteins. In this work we compared the kinetic folding mechanism of five p ostsynaptic density protein‐95, d isc‐large tumor suppressor protein, z onula occludens‐1 (PDZ) domains, sharing similar topology but having different primary structures. Investigation of the different proteins under various experimental conditions revealed that the folding kinetics of each member of the PDZ family can be described by a model with two transition states separated by an intermediate. Moreover, the positions of the two transition states along the reaction coordinate (as given by their β T ‐values) are fairly constant for the five PDZ domains." @default.
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• W2044713411 date "2007-02-15" @default.
• W2044713411 modified "2023-10-13" @default.
• W2044713411 title "A conserved folding mechanism for PDZ domains" @default.
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• W2044713411 doi "https://doi.org/10.1016/j.febslet.2007.02.011" @default.
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