Velocity-Dependent Mechanical Unfolding of Bacteriorhodopsin Is Governed by a Dynamic Interaction Network

摘要: Bacteriorhodopsin is a model system for membrane proteins. This seven transmembrane helical protein embedded within structure called purple membrane. Its structural stability against mechanical stress was recently investigated by atomic force microscopy experiments, in which single proteins were extracted from the Here, we study this process all-atom molecular dynamics simulations, bacteriorhodopsin molecules and unfolded an atomistic model. In our key features experiments like profiles location of residues that resist unfolding reproduced. These seen to be stabilized dynamic network intramolecular interactions. Further, pathway found velocity-dependent. Simulations released during revealed relaxation motions allowed characterization nonequilibrium processes fast extraction.