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- W2014611904 abstract "Dihydrofolate reductase mutants with amino acid replacements in the active center (Thr35-->Asp mutant, Arg57-->His mutant and the mutant with triple replacement Thr35-->Asp, Asn37-->Ser, Arg57-->His) were obtained by site-directed mutagenesis. The stabilization effect of trimethoprim and NADP.H on the protein tertiary structure in vitro has been investigated. In the case of mutants with a 'weak' tertiary structure (Thr35-->Asp35 and the triple mutant) the separate addition of ligands does not affect their stability. The simultaneous addition of these ligands to Thr35-->Asp35 and the triple mutant leads to the large increase in their stability. A distinct correlation was found between the in vitro studied stability of the mutant proteins to the urea- or heat-induced denaturation and the level of proteolytic degradation of these mutants previously observed in vivo." @default.
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- W2014611904 date "1993-01-01" @default.
- W2014611904 modified "2023-09-27" @default.
- W2014611904 title "Comparative stability of dihydrofolate reductase mutants <i>in vitro</i> and <i>in vivo</i>" @default.
- W2014611904 doi "https://doi.org/10.1093/protein/6.1.81" @default.
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