Dependence of protein mechanical unfolding pathways on pulling speeds.
Mechanical unfolding of the fourth domain of Distyostelium discoideum filamin (DDFLN4) was studied in detail using the C(alpha)-Go model. We show that unfolding pathways of this protein depend on the pulling speed. The agreement between theoretical and experimental results on the sequencing of unfolding events is achieved at low loading rates. The unfolding free energy landscape is also constructed using dependencies of unfolding forces on pulling speeds.
Institute of Physics, Polish Academy of Sciences, Aleja Lotnikow 32/46, 02-668 Warszawa, Poland. masli@ifpan.edu.pl
Mai Suan
MS
Li
Maksim
M
Kouza
D000818:Animals; D003198:Computer Simulation; D003285:Contractile Proteins / Q000737:chemistry*; D004023:Dictyostelium / Q000737:chemistry*; D064448:Filamins; D008840:Microfilament Proteins / Q000737:chemistry*; D008958:Models, Molecular; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D015800:Protozoan Proteins / Q000737:chemistry*; D013314:Stress, Mechanical
D003285:Contractile Proteins; D064448:Filamins; D008840:Microfilament Proteins; D015800:Protozoan Proteins