Folding and stretching in a Go-like model of titin.
Mechanical stretching of the I27 domain of titin and of its double and triple repeats are studied through molecular dynamics simulations of a Go-like model with Lennard-Jones contact interactions. We provide a thorough characterization of the system and correlate the sequencing of the folding and unraveling events with each other and with the contact order. The roles of cantilever stiffness and pulling rate are studied. Unraveling of tandem titin structures has a serial nature. The force-displacement curves in this coarse-grained model are similar to those obtained through all atom calculations.
Cieplak
Marek
M
Department of Physics and Astronomy, The Johns Hopkins University, Baltimore, Maryland, USA. mc@ifpan.edu.pl
Hoang
Trinh Xuan
TX
Robbins
Mark O
MO
D000818:Animals; D003198:Computer Simulation; D064211:Connectin; D007700:Kinetics; D008958:Models, Molecular; D015394:Molecular Structure; D009124:Muscle Proteins / Q000737:chemistry*; D017510:Protein Folding; D011494:Protein Kinases / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D013314:Stress, Mechanical; D013696:Temperature
D064211:Connectin; D009124:Muscle Proteins; D011494:Protein Kinases