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- W2024503780 abstract "Structural properties of two similar β-galactosidase fragments were investigated to determine how they influence the fragments' degradation rate in Escherichia coli. Both fragments resulting from a C-terminal nonsense mutation in lacZ, the CSH11 polypeptide and its 90 kDa degradative intermediate, exist predominantly as monomer subunits instead of in the tetrameric form characteristic of the native enzyme. However, both fragments appear to produce trace amounts of dimers and tetramers. The tetramer and higher molecular weight aggregates formed by the wild-type subunit confer greater protection for the enzyme's N-terminal auto-α polypeptide than does the monomer state of the β-galactosidase fragments. The thermally induced aggregation of both β-galactosidase fragments correlates with their sensitivity to α-chymotrypsin. The relatively low thermal stability of the 90 kDa degradative intermediate appears to be the cause of the significant increase in its proteolytic susceptibility at moderately high temperatures." @default.
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- W2024503780 date "1992-04-01" @default.
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- W2024503780 title "Structural characteristics of an abnormal protein influencing its proteolytic susceptibility" @default.
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- W2024503780 doi "https://doi.org/10.1016/0168-1656(92)90093-o" @default.
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