Role of conformational entropy in force-induced biopolymer unfolding.
A statistical mechanical description of flexible and semiflexible polymer chains in a poor solvent is developed in the constant force and constant distance ensembles. We predict the existence of many intermediate states at low temperatures stabilized by the force. A unified response to pulling and compressing forces has been obtained in the constant distance ensemble. We show the signature of a crossover length which increases linearly with the chain length. Below this crossover length, the critical force of unfolding decreases with temperature, while above, it increases with temperature. For stiff chains, we report for the first time sawtoothlike behavior in the force-extension curves which has been seen earlier in the case of protein unfolding.
Kumar
Sanjay
S
Department of Physics, Banaras Hindu University, Varanasi 221 005, India.
Jensen
Iwan
I
Jacobsen
Jesper L
JL
Guttmann
Anthony J
AJ
D000465:Algorithms; D019277:Entropy; D015233:Models, Statistical; D008968:Molecular Conformation; D011108:Polymers / Q000737:chemistry; D017510:Protein Folding; D012997:Solvents; D013696:Temperature; D013816:Thermodynamics
D011108:Polymers; D012997:Solvents