Titin force extension curves

Fig. 8. (a) Schematic of the AFM pulling experiments and expected unraveling of an individual nucleosome as a result of pulling on the DNA. (b) Example force-extension curves on isolated chicken erythrocyte chromatin fibers redrawn from Ref [69]. (c) Idealized schematic of a typical force-extension curve obtained on pulling single titin moleeules, as in the experiments of Rief et al. [71]. (d) Explanation of the titin force curve by successive unfolding of individual protein domains (see text). 

Figure 10.2 Single molecule force-extension curve of three different types of molecules (a) a short chain or rigid tod molecule (b) a long chain polymer with multiple domains, such as titin, where bi-b represents the unfolding of individual domains and (c) a tegular random coil long chain. Adapted from Smith et al. (1999). Copyright 1999 Nature Publishing Group.

Fig. 4. Predicted force extension curves of a single titin molecule in sarcomeres expressing cardiac titin isoforms or skeletal muscle isoforms.

Figure 4 Force-extension curves of titin-mimetic polypeptides, (a) (G-R)4 and (b) GRG5RG4R (G represents the GB1 domain and R represents the random-coil resilin domain). Reproduced with permission from Lv, S. Dudek, D. M. Cao, Y. etal. Nature 20 0, 465,69." Copyright 2010 Nature Publishing Group.

Figure 6 Three typical force extension curves obtained by stretching titin molecules. The curves show periodic structure on the retract portion of the data consistent with the unfolding of individual titin domains. Reproduced with permission from Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE (1997) Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276, 1109-1112.

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