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LARGE INCREASES IN GENERAL STABILITY FOR SUBTILISIN BPN(PRIME) THROUGH INCREMENTAL CHANGES IN THE FREE ENERGY OF UNFOLDING

NIAID Data Ecosystem2026-05-02 收录

蛋白质稳定性工程

酶热力学优化

数据链接：

https://www.rcsb.org/structure/1S01 数据链接链接失效反馈

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资源简介：

LARGE INCREASES IN GENERAL STABILITY FOR SUBTILISIN BPN(PRIME) THROUGH INCREMENTAL CHANGES IN THE FREE ENERGY OF UNFOLDING

应用场景：

创建时间：

2025-03-26

蛋白质稳定性工程

酶突变分析

STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY CAVITY-FILLING MUTATIONS WITHIN A HYDROPHOBIC CORE Descriptor: RIBONUCLEASE H Authors: Ishikawa, K, Nakamura, H, Morikawa, K, Kanaya, S. Deposit da

Protein Data Bank Japan2024-02-14 更新40

An ultra-stable single-chain insulin analog resists thermal inactivation and exhibits biological signaling duration equivalent to the native protein

胰岛素类似物

蛋白质稳定性工程

An ultra-stable single-chain insulin analog resists thermal inactivation and exhibits biological signaling duration equivalent to the native protein Descriptor: Single-chain insulin analog Authors: Ye

Protein Data Bank Japan2024-11-06 更新20

Schistosoma mansoni Sm14 Fatty Acid-Binding Protein: improvement of protein stability by substitution of the single Cys62 residue

蛋白质稳定性工程

血吸虫疫苗开发

Schistosoma mansoni Sm14 Fatty Acid-Binding Protein: improvement of protein stability by substitution of the single Cys62 residue Descriptor: 14 kDa fatty acid-binding protein Authors: Ramos, C.R.R, O

Protein Data Bank Japan2024-05-15 更新10

Stabilization of PYR1 Biosensors by GMMA

生物传感器

蛋白质稳定性工程

Functional screens were used in conjunction with GMMA to identify universally stabilizing mutations for the biosensor PYR1.

NIAID Data Ecosystem40

Stability of leucine zipper-TRAIL fusion proteins.

蛋白质稳定性工程

肿瘤凋亡诱导剂

The ratio of dead cells was determined as described in the legend for Table 2. Residual cytotoxic activity of the TRAIL samples after 20 min treatment at 70°C was calculated for 3 and 10 μl of 100-fol

Figshare2015-12-03 更新20

LARGE INCREASES IN GENERAL STABILITY FOR SUBTILISIN BPN(PRIME) THROUGH INCREMENTAL CHANGES IN THE FREE ENERGY OF UNFOLDING

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