On the Extension Behavior of Helicogenic Polypeptides

Details On the Extension Behavior of Helicogenic Polypeptides On the Extension Behavior of Helicogenic Polypeptides

2001-12-13

arxiv.org/abs/cond-mat/0112246v1

Macromolecules 35, 3238-3252 (2002)

Physics

Condensed Matter

Soft Condensed Matter

18 pages, 10 figures, to be published in Macromolecules

Scientific paper

10.1021/ma011631w

The force laws governing the extension behavior of homopolypeptides are obtained from a phenomenological free energy capable of describing the helix-coil transition. Just above the melting temperature of the free chains, T*, the plot of force, f, vs. end-to-end distance, R, exhibits two plateaus associated with coexistence of helical and coil domains. The lower plateau is due to tension induced onset of helix-coil transition. The higher plateau corresponds to the melting of the helices by overextension. Just below T* the f-R plot exhibits only the upper plateau. The f-R plots, the helical fraction, the number of domains and their polydispersity are calculated for two models: In one the helical domains are viewed as rigid rods while in the second they are treated as worm like chains.

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