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Mechanical stretching of proteins: calmodulin and titin

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  • Cieplak, Marek

Abstract

Mechanical unfolding of several domains of calmodulin and titin is studied using a Go-like model with a realistic contact map and Lennard–Jones contact interactions. It is shown that this simple model captures the experimentally observed difference between the two proteins: titin is a spring that is tough and strong whereas calmodulin acts like a weak spring with featureless force–displacement curves. The difference is related to the dominance of the α secondary structures in the native structure of calmodulin. The tandem arrangements of calmodulin unwind simultaneously in each domain whereas the domains in titin unravel in a serial fashion. The sequences of contact events during unravelling are correlated with the contact order, i.e., with the separation between contact making amino acids along the backbone in the native state. Temperature is found to affect stretching in a profound way.

Suggested Citation

  • Cieplak, Marek, 2005. "Mechanical stretching of proteins: calmodulin and titin," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 352(1), pages 28-42.
    • Handle: RePEc:eee:phsmap:v:352:y:2005:i:1:p:28-42
    DOI: 10.1016/j.physa.2004.12.032
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    1. Catherine A. Maritan & Thomas H. Brush, 2003. "Heterogeneity and transferring practices: implementing flow manufacturing in multiple plants," Strategic Management Journal, Wiley Blackwell, vol. 24(10), pages 945-959, October.
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