Thermal unfolding of proteins.
Thermal unfolding of proteins is compared to folding and mechanical stretching in a simple topology-based dynamical model. We define the unfolding time and demonstrate its low-temperature divergence. Below a characteristic temperature, contacts break at separate time scales and unfolding proceeds approximately in a way reverse to folding. Features in these scenarios agree with experiments and atomic simulations on titin.
Cieplak
Marek
M
Institute of Physics, Polish Academy of Sciences, Aleja Lotników 32/46, 02-668 Warsaw, Poland. mc@ifpan.edu.pl
Sułkowska
Joanna I
JI
D002627:Chemistry, Physical / Q000379:methods*; D003198:Computer Simulation; D064211:Connectin; D007700:Kinetics; D008958:Models, Molecular; D008968:Molecular Conformation; D009124:Muscle Proteins / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011494:Protein Kinases / Q000737:chemistry; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013696:Temperature; D013997:Time Factors
D064211:Connectin; D009124:Muscle Proteins; D011506:Proteins; D011494:Protein Kinases