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coli variants with the Thr35 Asp and Thr35 Asp/Asn37 Ser/Arg57 His mutations in the active site were compact and have pronounced secondary structure, they did not possess rigid 3D structure and were 10 times more susceptible to limited trypsinolysis in comparison with the wild type protein, emphasizing low proteolytic stability of these intrinsically disordered molten globular mutants (Leontiev et al., 1993)

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doi: 10.1111/j.1365-2982.2012.01891.x 201 KomaroffALLipkinWI