The unique topology of the B1 immunoglobulin G (IgG) binding domain of streptococcal protein G (GB1) leads to its remarkable mechanical stability. This nonmechanical protein is shown to be mechanically stable and to unfold at about 180 pN (the force-extension curves (right) shown demonstrate the mechanical unraveling of each GB1 domain in the polyprotein which is made of direct tandem repeats of GB1 (left)).
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Cao et al. (2005) studied this question.
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