Abstract
We introduced new termini on surface loops of green fluorescent protein (GFP) by linking the original ones. The mechanical properties of two circularly permuted GFPs (cpGFPs) were examined by atomic force microscopy (AFM) and compared with those of the base GFPs. The unfolding results revealed different levels of the reduced mechanical stability of cpGFPs, and these levels were related to the proximity of the newly introduced termini to the central `β-can'.
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