Physics – Condensed Matter – Soft Condensed Matter
Scientific paper
1999-05-25
Proc. Natl. Acad. Sci. USA, vol. 96, pp. 6166-6170 (1999)
Physics
Condensed Matter
Soft Condensed Matter
12 pages, Latex, 6 ps figures
Scientific paper
10.1073/pnas.96.11.6166
Single molecule force spectroscopy reveals unfolding of domains in titin upon stretching. We provide a theoretical framework for these experiments by computing the phase diagrams for force-induced unfolding of single domain proteins using lattice models. The results show that two-state folders (at zero force) unravel cooperatively whereas stretching of non-two-state folders occurs through intermediates. The stretching rates of individual molecules show great variations reflecting the heterogeneity of force-induced unfolding pathways. The approach to the stretched state occurs in a step-wise "quantized" manner. Unfolding dynamics depends sensitively on topology. The unfolding rates increase exponentially with force f till an optimum value which is determined by the barrier to unfolding when f=0. A mapping of these results to proteins shows qualitative agreement with force-induced unfolding of Ig-like domains in titin. We show that single molecule force spectroscopy can be used to map the folding free energy landscape of proteins in the absence of denaturants.
Klimov D. K.
Thirumalai Dave
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