|Title||Extending a Spectrin Repeat Unit. II: Rupture Behavior|
|Publication Type||Journal Article|
|Year of Publication||2006|
|Authors||Paramore, S, Ayton, GS, Voth, GA|
|Keywords||Animals Brain/metabolism Chickens Computer Simulation Hydrogen Bonding Microscopy, Atomic Force Models, Molecular Molecular Conformation Protein Conformation Protein Denaturation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Software Spectrin/*chemistry Time Factors|
A spectrin repeat unit was subject to extension using cyclic expansion nonequilibrium molecular dynamics. Periodic boundary conditions were used to examine the effects of the contiguous alpha-helical linker on the force response. The measured force-extension curve shows a linear increase in the force response when the spectrin repeat unit is extended by approximately 0.4 nm. After that point, the force response peaks and subsequently declines. The peak in the force response marks the point where the spectrin repeat unit undergoes a change in its material properties from a strongly elastic material to a mostly viscous one, on the timescales of the simulations. The force peak is also correlated with rupture of the alpha-helical linker, and is likely the event responsible for the peaks in the sawtooth-pattern force-extension curves measured by atomic force microscopy experiments. Rupture of the linker involves simultaneously breaking approximately four hydrogen bonds that maintain the alpha-helical linker. After this initial rupture, the linker undergoes simple helix-to-coil transitions as the spectrin repeat unit continues to be extended. The implications of linker rupture in the interpretation of unfolding and atomic force microscopy experiments are also discussed.