Mechanical Stretching of Proteins: Calmodulin and Titin

Details Mechanical Stretching of Proteins: Calmodulin and Titin Mechanical Stretching of Proteins: Calmodulin and Titin

2004-12-16

arxiv.org/abs/q-bio/0412032v1

Biology

Quantitative Biology

Biomolecules

To be published in a special bio-issue of Physica A; 14 figures

Scientific paper

10.1016/j.physa.2004.12.032

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 alpha 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 unraveling 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.

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