ProThermDB（Thermodynamic Database for Proteins and Mutants）是一个蛋白质及其突变体热力学数据库，由印度理工学院马德拉斯分校开发维护。该数据库收录蛋白稳定性相关的实验热力学参数（如熔解温度、自由能、焓变等），并结合序列、结构、实验条件及文献信息，支持蛋白质稳定性与突变效应研究。

知名数据库4860

File S1 - The Key to the Extraordinary Thermal Stability of P. furiosus Holo-Rubredoxin: Iron Binding-Guided Packing of a Core Aromatic Cluster Responsible for High Kinetic Stability of the Native Structure

蛋白质力学稳定性

铁结合蛋白结构研究

Supporting information and figures. Figure S1, Panel a : Control solutions lacking ferrozine. Tube-1 contains a ferric chloride solution. Tube-2 contains ferric chloride and beta-mercaptoethanol. Tube

NIAID Data Ecosystem100

Global Analysis of Protein Folding Thermodynamics for Disease State Characterization

蛋白质力学稳定性

乳腺癌分子标志物发现

Current methods for the large-scale characterization of disease states generally rely on the analysis of gene and/or protein expression levels. These existing methods fail to detect proteins with dise

NIAID Data Ecosystem50

Protein Aggregation: Kinetics versus Thermodynamics

蛋白质聚集动力学

蛋白质力学稳定性

In this study, we address the questions of how important is the kinetics in protein aggregation, and what are the intrinsic properties of proteins that cause this behavior. On the basis of our recent

NIAID Data Ecosystem110

Thermodynamic stability of de novo designed protein mini-binders as assessed by combined thermal and chemical denaturation - Data set

蛋白质力学稳定性

从头设计蛋白质分析

Experimental data for the paper: "Global analysis of thermal and chemical denaturation using CheMelt: Thermodynamic dissection of highly thermostable de novo designed proteins" by Vili Lampinen; Osval

NIAID Data Ecosystem60