Switch from thermal to force-driven pathways of protein refolding.

Abstract

The impact of the quenched force on protein folding pathways and free energy landscape was studied in detail. Using the coarse-grain Go model, we have obtained the low, middle, and high force regimes for protein refolding under the quenched force. The folding pathways in the low force regime coincide with the thermal ones. A clear switch from thermal folding pathways to force-driven pathways in the middle force regime was observed. The distance between the denatured state and transition state xf in the temperature-driven regime is smaller than in the force-driven one. The distance xf obtained in the middle force regime is consistent with the available experimental data suggesting that atomic force microscopy experiments deal with the force-regime which is just above the thermal one.