CHalf: Folding Stability Made Simple

Chad D. Hyer

doi:10.1021/acs.jproteome.2c00619

2023-01-27

PRE

DOI：10.1021/acs.jproteome.2c00619

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摘要

En 中文

The structure of a protein defines its function and integrity and correlates with the protein folding stability (PFS). Quantifying PFS allows researchers to assess differential stability of proteins in different disease or ligand binding states, providing insight into protein efficacy and potentially serving as a metric of protein quality. There are a number of mass spectrometry (MS)based methods to assess PFS, such as (T) under bar hermal (P) under bar rotein (P) under bar rofiling (TPP), (S) under bar tability of (P) under bar roteins from (R) under bar ates of (Ox) under bar idation (SPROX), and (I) under bar odination (P) under bar rotein (S) under bar tability (A) under bar ssay (IPSA). Despite the critical value that PFS studies add to the understanding of mechanisms of disease and treatment development, proteomics research is still primarily dominated by concentration-based studies. We found that a major reason for the lack of PFS studies is the lack of a userfriendly data processing tool. Here we present the first user-friendly software, C-Half, with a graphical user interface for calculating PFS. Besides calculating site-specific PFS of a given protein from chemical denature folding stability assays, C-Half is also compatible with thermal denature folding stability assays. C-Half also includes a set of data visualization tools to help identify changes in PFS across protein sequences and in between different treatment conditions. We expect the introduction of C-Half to lower the barrier of entry for researchers to investigate PFS, promoting the usage of PFS in studies. In the long run, we expect this increase in PFS research to accelerate our understanding of the pathogenesis and pathophysiology of disease.

Keyword:

protein folding stability

TPP

SPROX

IPSA

graphical user interface

期刊

Journal of Proteome Research

IF:

3.6

论文数:

9.4K

被引数:

2.3W

机构

Brigham Young University

学者数:

9.0K

论文数: 6.0K

被引数: 9.3K

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