title: 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 xfin the temperature-driven regime is smaller than in the force-driven one. The distance xfobtained 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.
authors.affiliation: Faculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland.
authors.forename: Maksim
authors.identifier: 0000000217049797
authors.initials: M
authors.lastname: Kouza
authors.affiliation: Institute for Computational Science and Technology, Tan Chanh Hiep Ward, District 12, Ho Chi Minh City, Vietnam and Department of Theoretical Physics, Faculty of Physics and Engineering Physics, Ho Chi Minh University of Science, Vietnam.
authors.forename: Pham Dang
authors.initials: PD
authors.lastname: Lan
authors.affiliation: Institute of Physics, National Academy of Sciences of Ukraine, 46, Nauka Ave., Kyiv 03680, Ukraine.
authors.forename: Alexander M
authors.initials: AM
authors.lastname: Gabovich
authors.affiliation: Faculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland.
authors.forename: Andrzej
authors.initials: A
authors.lastname: Kolinski
authors.affiliation: Institute of Physics, Polish Academy of Science, Al. Lotnikow 32/46, 02-668 Warsaw, Poland.
authors.forename: Mai Suan
authors.identifier: 0000000170217916
authors.initials: MS
authors.lastname: Li
mesh_terms: D008956:Models, Chemical; D056004:Molecular Dynamics Simulation; D055585:Physical Phenomena; D011489:Protein Denaturation; D058849:Protein Refolding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins