The kinetic were acquired in vitro with purified proteins. The Tm and m values (indicating the cooperativity of unfolding) were extracted from heat denaturation. N.D.; not determined. Errors shown are

NIAID Data Ecosystem30

Thermal stability of WT and mutants of the c-Src-SH3 domain.

蛋白质热稳定性

结构域突变分析

aErrors are fitting errors to the two-state denaturation model.Thermal stability of WT and mutants of the c-Src-SH3 domain.

Figshare2015-12-02 更新20

Thermal stability parameters for holo and apo SpFld.

蛋白质热稳定性

生物生理研究

Thermal stability parameters for holo and apo SpFld.

Figshare2016-09-21 更新30

THERMOSTABLE PROTEIN FROM HYPERTHERMOPHILIC VIRUS SSV-RH

蛋白质热稳定性

超嗜热病毒生物学

THERMOSTABLE PROTEIN FROM HYPERTHERMOPHILIC VIRUS SSV-RH

NIAID Data Ecosystem20

Tm values of PRC1-DD and its mutants.

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