用于原位绘制蛋白质复合物拓扑结构的交联质谱。

IF 5.6 2区生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY

Essays in biochemistry Pub Date : 2023-03-29 DOI:10.1042/EBC20220168

Kitaik Lee, Francis J O'Reilly

{"title":"用于原位绘制蛋白质复合物拓扑结构的交联质谱。","authors":"Kitaik Lee, Francis J O'Reilly","doi":"10.1042/EBC20220168","DOIUrl":null,"url":null,"abstract":"Cross-linking mass spectrometry has become an established technology to provide structural information on the topology and dynamics of protein complexes. Readily accessible workflows can provide detailed data on simplified systems, such as purified complexes. However, using this technology to study the structure of protein complexes in situ, such as in organelles, cells, and even tissues, is still a technological frontier. The complexity of these systems remains a considerable challenge, but there have been dramatic improvements in sample handling, data acquisition, and data processing. Here, we summarise these developments and describe the paths towards comprehensive and comparative structural interactomes by cross-linking mass spectrometry.","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":"67 2","pages":"215-228"},"PeriodicalIF":5.6000,"publicationDate":"2023-03-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10070479/pdf/","citationCount":"0","resultStr":"{\"title\":\"Cross-linking mass spectrometry for mapping protein complex topologies in situ.\",\"authors\":\"Kitaik Lee, Francis J O'Reilly\",\"doi\":\"10.1042/EBC20220168\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Cross-linking mass spectrometry has become an established technology to provide structural information on the topology and dynamics of protein complexes. Readily accessible workflows can provide detailed data on simplified systems, such as purified complexes. However, using this technology to study the structure of protein complexes in situ, such as in organelles, cells, and even tissues, is still a technological frontier. The complexity of these systems remains a considerable challenge, but there have been dramatic improvements in sample handling, data acquisition, and data processing. Here, we summarise these developments and describe the paths towards comprehensive and comparative structural interactomes by cross-linking mass spectrometry.\",\"PeriodicalId\":11812,\"journal\":{\"name\":\"Essays in biochemistry\",\"volume\":\"67 2\",\"pages\":\"215-228\"},\"PeriodicalIF\":5.6000,\"publicationDate\":\"2023-03-29\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10070479/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Essays in biochemistry\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1042/EBC20220168\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Essays in biochemistry","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1042/EBC20220168","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}

引用次数: 0

摘要

交联质谱技术已成为提供蛋白质复合物拓扑和动态结构信息的成熟技术。随时可用的工作流程可提供简化系统（如纯化复合物）的详细数据。然而，利用这种技术研究原位蛋白质复合物的结构，如细胞器、细胞甚至组织中的复合物，仍然是一个技术前沿。这些系统的复杂性仍然是一个相当大的挑战，但在样品处理、数据采集和数据处理方面已经取得了巨大的进步。在此，我们总结了这些进展，并描述了通过交联质谱技术实现全面、可比较的结构相互作用组的途径。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Cross-linking mass spectrometry for mapping protein complex topologies in situ.

查看原文本刊更多论文

Cross-linking mass spectrometry for mapping protein complex topologies in situ.

Cross-linking mass spectrometry has become an established technology to provide structural information on the topology and dynamics of protein complexes. Readily accessible workflows can provide detailed data on simplified systems, such as purified complexes. However, using this technology to study the structure of protein complexes in situ, such as in organelles, cells, and even tissues, is still a technological frontier. The complexity of these systems remains a considerable challenge, but there have been dramatic improvements in sample handling, data acquisition, and data processing. Here, we summarise these developments and describe the paths towards comprehensive and comparative structural interactomes by cross-linking mass spectrometry.

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

Essays in biochemistry 生物-生化与分子生物学

CiteScore

10.50

自引率

0.00%

发文量

105

审稿时长

>12 weeks

期刊介绍： Essays in Biochemistry publishes short, digestible reviews from experts highlighting recent key topics in biochemistry and the molecular biosciences. Written to be accessible for those not yet immersed in the subject, each article is an up-to-date, self-contained summary of the topic. Bridging the gap between the latest research and established textbooks, Essays in Biochemistry will tell you what you need to know to begin exploring the field, as each article includes the top take-home messages as summary points. Each issue of the journal is guest edited by a key opinion leader in the area, and whether you are continuing your studies or moving into a new research area, the Journal gives a complete picture in one place. Essays in Biochemistry is proud to publish Understanding Biochemistry, an essential online resource for post-16 students, teachers and undergraduates. Providing up-to-date overviews of key concepts in biochemistry and the molecular biosciences, the Understanding Biochemistry issues of Essays in Biochemistry are published annually in October.