Predicted changes in stability as a result of mutation.

NIAID Data Ecosystem2026-05-01 收录

蛋白质稳定性

突变效应评估

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https://figshare.com/articles/dataset/Predicted_changes_in_stability_as_a_result_of_mutation_/23525817 数据链接链接失效反馈

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资源简介：

Predicted changes in stability as a result of mutation.

创建时间：

2023-06-15

Simulation results on non-DHFR proteins.

蛋白质稳定性

计算生物学

Design of proteins with desired thermal properties is important for scientific and biotechnological applications. Here we developed a theoretical approach to predict the effect of mutations on protein

NIAID Data Ecosystem60

CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

蛋白质稳定性

疏水效应

CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME Descriptor: LYSOZYME, SODIUM ION Authors: Takano, K, Yamagata, Y, Yutani, K. Deposit date: 1998-05-21 Release date:

Protein Data Bank Japan2024-11-20 更新40

BURIED POLAR MUTANT HUMAN LYSOZYME

蛋白质稳定性

X射线晶体学

BURIED POLAR MUTANT HUMAN LYSOZYME Descriptor: LYSOZYME, SODIUM ION Authors: Takano, K, Yamagata, Y, Yutani, K. Deposit date: 2000-11-30 Release date: 2001-04-18 Last modified: 2024-11-13 Method: X-RA

Protein Data Bank Japan2024-11-13 更新30

Increase in the thermostability of Bacillus sp. strain TAR-1 xylanase using a site saturation mutagenesis library

酶工程

蛋白质稳定性

Site saturation mutagenesis library is a recently developed technique, in which any one out of all amino acid residues in a target region is substituted into other 19 amino acid residues. In this stud

NIAID Data Ecosystem40

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V74A MUTANT

蛋白质稳定性

X射线晶体学

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V74A MUTANT Descriptor: LYSOZYME, SODIUM ION Authors: Takano, K, Yamagata, Y, Fujii, S, Yutani, K. Depos

Protein Data Bank Japan2024-11-06 更新30

Predicted changes in stability as a result of mutation.

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