首页/数据集/Transition temperatures (Tm) for thermal denaturation of the wild-type and mutant Sfβgly proteins.

Transition temperatures (Tm) for thermal denaturation of the wild-type and mutant Sfβgly proteins.

NIAID Data Ecosystem2026-03-08 收录

蛋白质热变性分析

蛋白质稳定性评估

数据链接：

https://figshare.com/articles/dataset/_Transition_temperatures_T_m_for_thermal_denaturation_of_the_wild_type_and_mutant_Sf_946_gly_proteins_/1019590 数据链接链接失效反馈

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Standard deviations were lower than 0.5 K.

应用场景：

创建时间：

2014-05-07

单克隆抗体修饰分析

蛋白质稳定性评估

Relative quantification (in %) was conducted by specific ion current chromatogram analysis of proteolytic peptides (LysC or trypsin) using the quantification software GRAMS/32™ (n = 2, mean ± S.D). MA

Figshare2015-12-02 更新20

Thermodynamic parameters associated with the thermal unfolding of lysozyme and RNase-A in the presence of different concentrations of urea- NaCl mixture at pH 7.0.

蛋白质热变性分析

生化实验

Thermodynamic parameters associated with the thermal unfolding of lysozyme and RNase-A in the presence of different concentrations of urea- NaCl mixture at pH 7.0.

NIAID Data Ecosystem20

Isoelectric point determination and thermal unfolding monitored by circular dichroism.

蛋白质等电点测定

蛋白质热变性分析

Isoelectric point determination and thermal unfolding monitored by circular dichroism.

NIAID Data Ecosystem10

Parameter values obtained upon fitting the circular dichroism thermal unfolding curves (ellipticity at 206 nm, Fig. 12A; ellipticity at 283 nm, Fig. 12B) of human plasminogen with a modified Boltzmann function.

蛋白质热变性分析

圆二色光谱应用

NIAID Data Ecosystem20

pH stability of e- and pCTB determined by TSAa.

蛋白质稳定性评估

pH依赖性分析

aProteins were diluted in appropriate pH buffers (see Experimental Procedures for details).bTm were determined by the vertex of the first derivative of the relative fluorescence unit values. The assay

Figshare2015-12-02 更新20

Transition temperatures (<i>T</i><sub>m</sub>) for thermal denaturation of the wild-type and mutant Sfβgly proteins.

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