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- W1982329305 abstract "Using DSC, the thermal unfolding of RNase A, RNase B, and two partly deglycosylated RNase B forms was studied. The oligosaccharide side chain leads to slight protein stabilization. The conformational stability at pH 4.0 amounts to ΔG25°C=34.5, 34.6, 33.7, and 32.8 kJ mol−1 for RNase B, Man1-RNase, GlnNAc1-RNase, and RNase A, respectively. The heat capacity remains the same for glycosylated and deglycosylated protein. These results are consistent with a proposed hydrogen bond of Lys37 with GlnNAc-1." @default.
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- W1982329305 date "2002-01-01" @default.
- W1982329305 modified "2023-09-23" @default.
- W1982329305 title "The influence of glycosylation on the thermal stability of ribonuclease" @default.
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- W1982329305 doi "https://doi.org/10.1016/s0040-6031(01)00727-4" @default.
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