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引用次数: 0
摘要
热蛋白质组分析(TPP)是一项创新技术,它利用蛋白质热稳定性原理来识别潜在的蛋白质相互作用伙伴。TPP 采用定量质谱法测量整个蛋白质组的蛋白质稳定性,在一次实验中提供蛋白质相互作用的全面快照。在研究蛋白质-蛋白质相互作用(PPI)时,TPP 利用表观蛋白质熔解温度的变化来识别大多数传统 PPI 检测方法难以测量的瞬时弱相互作用。本综述讨论了当前的 TPP 方法、解读由此产生的复杂数据集所面临的挑战以及深化和改进 PPI 网络的机会。通过推进我们对错综复杂的蛋白质相互作用的掌握,TPP有望阐明疾病的分子基础并推动新型治疗靶点的发现。
Characterizing protein-protein interactions with thermal proteome profiling
Thermal proteome profiling (TPP) is an innovative technique that uses the principle of protein thermal stability to identify potential protein interaction partners. Employing quantitative mass spectrometry, TPP measures protein stability across the proteome, offering a comprehensive snapshot of protein interactions in a single experiment. When studying protein-protein interactions (PPI), TPP leverages changes in apparent protein melting temperatures to identify transient and weak interactions that most traditional PPI detection methodologies struggle to measure. This review discusses current TPP methodologies, the challenges of interpreting the resulting complex datasets, and opportunities to deepen and improve PPI networks. By advancing our grasp of intricate protein interactions, TPP promises to illuminate the molecular basis of diseases and drive the discovery of novel therapeutic targets.
期刊介绍:
Current Opinion in Structural Biology (COSB) aims to stimulate scientifically grounded, interdisciplinary, multi-scale debate and exchange of ideas. It contains polished, concise and timely reviews and opinions, with particular emphasis on those articles published in the past two years. In addition to describing recent trends, the authors are encouraged to give their subjective opinion of the topics discussed.
In COSB, we help the reader by providing in a systematic manner:
1. The views of experts on current advances in their field in a clear and readable form.
2. Evaluations of the most interesting papers, annotated by experts, from the great wealth of original publications.
[...]
The subject of Structural Biology is divided into twelve themed sections, each of which is reviewed once a year. Each issue contains two sections, and the amount of space devoted to each section is related to its importance.
-Folding and Binding-
Nucleic acids and their protein complexes-
Macromolecular Machines-
Theory and Simulation-
Sequences and Topology-
New constructs and expression of proteins-
Membranes-
Engineering and Design-
Carbohydrate-protein interactions and glycosylation-
Biophysical and molecular biological methods-
Multi-protein assemblies in signalling-
Catalysis and Regulation