热稳定性
蛋白质组
化学
小分子
计算生物学
核酸
蛋白质组学
质谱法
热休克蛋白90
生物化学
生物
色谱法
热休克蛋白
酶
基因
作者
Yanhua Qiu,Bintao Zhai,Yubin Bai,Shulin Chen,Jiyu Zhang
出处
期刊:PubMed
日期:2022-10-25
卷期号:38 (10): 3628-3637
标识
DOI:10.13345/j.cjb.220206
摘要
Thermal proteome profiling (TPP) is a combination of cellular thermal shift assay (CETSA) and quantitative mass spectrometry (MS), also termed as MS-CETSA. TPP determines the stability of the entire proteome by measuring the content of soluble proteins in cells or cell lysates at different heating temperatures. Proteins can change their thermostability when interacting with small molecules (e.g., drugs or metabolites), nucleic acids, or other proteins or posttranslational modification, while TPP can identify target proteins based on the difference in thermostability with or without ligand-binding. At present, TPP has been applied to identify the targets and off-targets of drugs and interrogate protein-metabolite and protein-protein interactions. Due to limited understanding of this technology, this review introduced the principles, methods, applications, advantages and limitations of TPP.
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