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. 2002 Apr;11(4):806–819. doi: 10.1110/ps.3510102

Table 2.

Alanine mutants of BPTI used in the study

Lys15Arg R15 80%a
Pro13Ala, Lys15Arg A13R15 70%a
Thr11Ala, Pro13Ala, Lys15Arg A11A13R15 60%a
Lys15Arg, Arg17Ala R15A17 70%a
Lys15Arg, Val34Ala R15A34 70%a
Lys15Arg, Val34Ala, Gly37Ala, Arg39Ala R15A34A37A39 40%a
Pro13Ala, Lys15Arg, Arg17Ala, Ile18Ala, Ile19Ala A13R15A17A18A19 40%a
Thr11Ala, Pro13Ala, Lys15Arg, Arg17Ala, Ile18Ala, Ile19Ala A11A13R15A17A18A19 30%a
Pro13Ala, Lys15Arg, Arg17Ala, Ile18Ala, Ile19Ala, Val34Ala A13R15A17A18A19A34 30%b
Thr11Ala, Pro13Ala, Lys15Arg, Arg17Ala, Ile18Ala, Ile19Ala, Val34Ala A11A13R15A17A18A19A34 30%b
Thr11Ala, Pro13Ala, Lys15Arg, Arg17Ala, Ile18Ala, Ile19Ala, Val34Ala, Gly37Ala, Arg39Ala A11A13R15A17A18A19A34A37A39 30%b

Alanine mutations introduced into the primary binding loop are shown in bold and those in the secondary binding loop are in italic. All mutants contain additional Met52Leu substitution. Refolding yield is shown in the third column.

a Refolding conditions: 1 × 10−4 M BTPI, 4 M urea, 20 mM Tris, pH 8.7, 6 × 10−4 M GSH, 3 × 10−4 M

GSSG, 3 mM EDTA, 1 h, 47°C.

b Refolding conditions: 1 × 10−5 M BPTI, 0.4 M urea, 20 mM Tris, pH 8.7, 6 × 10−4 M GSH, 3 × 10−4 M GSSG, 3 mM EDTA, 1 h, 37°C.