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Mechanical stretching of six proteins is studied through molecular dynamicssimulations. The model is Go-like, with Lennard-Jones interactions at nativecontacts. Low temperature unfolding scenarios are remarkably complex andsensitive to small structural changes. Thermal fluctuations reduce the peakforces and the number of metastable states during unfolding. The unfoldingpathways also simplify as temperature rises. In the entropic limit, allproteins show a monotonic decrease of the extension where bonds rupture withtheir separation along the backbone (contact order).Comment: RevTex, 5 pages, 5 figures, to appear in Phys. Rev.

Stretching of proteins in the entropic limit