Joining Forces: Integrating Proteomics and Cross-linking with the Mass Spectrometry of Intact Complexes

被引:53
|
作者
Stengel, Florian [1 ,2 ]
Aebersold, Ruedi [2 ,3 ]
Robinson, Carol V. [1 ]
机构
[1] Univ Oxford, Chem Res Lab, Oxford OX1 3TA, England
[2] Inst Mol Syst Biol, CH-8093 Zurich, Switzerland
[3] Univ Zurich, Fac Sci, Zurich, Switzerland
关键词
PROTEIN COMPLEXES; GAS-PHASE; SUBUNIT ARCHITECTURE; ELECTROSPRAY-IONIZATION; ESCHERICHIA-COLI; ABSOLUTE QUANTIFICATION; DISSOCIATION PATHWAYS; STRUCTURAL-ANALYSIS; BAC TRANSGENEOMICS; 26S PROTEASOME;
D O I
10.1074/mcp.R111.014027
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Protein assemblies are critical for cellular function and understanding their physical organization is the key aim of structural biology. However, applying conventional structural biology approaches is challenging for transient, dynamic, or polydisperse assemblies. There is therefore a growing demand for hybrid technologies that are able to complement classical structural biology methods and thereby broaden our arsenal for the study of these important complexes. Exciting new developments in the field of mass spectrometry and proteomics have added a new dimension to the study of protein-protein interactions and protein complex architecture. In this review, we focus on how complementary mass spectrometry-based techniques can greatly facilitate structural understanding of protein assemblies. Molecular & Cellular Proteomics 11: 10.1074/mcp.R111.014027, 1-13, 2012.
引用
收藏
页数:13
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