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Issue 20, 2009
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Free energies and forces in helix–coil transition of homopolypeptides under stretching

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Abstract

We show here that constant velocity steered molecular dynamics (SMD) simulations of α-helices in a vacuum present a well defined plateau in the force–extension relationship for homopolypeptides having more than (approximately) twenty residues. With the processes being far away from equilibrium, the energies strongly depend on the stretching velocity. Importantly, for a given velocity variation, the energy variation depends also on the helix sequence. Additionally, our observations show that homopolypeptides made of ten different amino acids (Ala, Cys, Gln, Ile, Leu, Met, Phe, Ser, Thr and Val) present a linear helix–coil transition.

Graphical abstract: Free energies and forces in helix–coil transition of homopolypeptides under stretching

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Publication details

The article was received on 10 Nov 2008, accepted on 06 Feb 2009 and first published on 06 Mar 2009


Article type: Paper
DOI: 10.1039/B820021A
Citation: Phys. Chem. Chem. Phys., 2009,11, 4019-4024

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    Free energies and forces in helix–coil transition of homopolypeptides under stretching

    F. C. Zegarra, G. N. Peralta, A. M. Coronado and Y. Q. Gao, Phys. Chem. Chem. Phys., 2009, 11, 4019
    DOI: 10.1039/B820021A

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