Your browser doesn't support javascript.
loading
Interfaces with Structure Dynamics of the Workhorses from Cells Revealed through Cross-Linking Mass Spectrometry (CLMS).
Kalathiya, Umesh; Padariya, Monikaben; Faktor, Jakub; Coyaud, Etienne; Alfaro, Javier A; Fahraeus, Robin; Hupp, Ted R; Goodlett, David R.
Affiliation
  • Kalathiya U; International Centre for Cancer Vaccine Science, University of Gdansk, ul. Kladki 24, 80-822 Gdansk, Poland.
  • Padariya M; International Centre for Cancer Vaccine Science, University of Gdansk, ul. Kladki 24, 80-822 Gdansk, Poland.
  • Faktor J; International Centre for Cancer Vaccine Science, University of Gdansk, ul. Kladki 24, 80-822 Gdansk, Poland.
  • Coyaud E; Protéomique Réponse Inflammatoire Spectrométrie de Mass-PRISM, Inserm U1192, University Lille, CHU Lille, F-59000 Lille, France.
  • Alfaro JA; International Centre for Cancer Vaccine Science, University of Gdansk, ul. Kladki 24, 80-822 Gdansk, Poland.
  • Fahraeus R; Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, Scotland EH4 2XR, UK.
  • Hupp TR; International Centre for Cancer Vaccine Science, University of Gdansk, ul. Kladki 24, 80-822 Gdansk, Poland.
  • Goodlett DR; International Centre for Cancer Vaccine Science, University of Gdansk, ul. Kladki 24, 80-822 Gdansk, Poland.
Biomolecules ; 11(3)2021 03 04.
Article in En | MEDLINE | ID: mdl-33806612
ABSTRACT
The fundamentals of how protein-protein/RNA/DNA interactions influence the structures and functions of the workhorses from the cells have been well documented in the 20th century. A diverse set of methods exist to determine such interactions between different components, particularly, the mass spectrometry (MS) methods, with its advanced instrumentation, has become a significant approach to analyze a diverse range of biomolecules, as well as bring insights to their biomolecular processes. This review highlights the principal role of chemistry in MS-based structural proteomics approaches, with a particular focus on the chemical cross-linking of protein-protein/DNA/RNA complexes. In addition, we discuss different methods to prepare the cross-linked samples for MS analysis and tools to identify cross-linked peptides. Cross-linking mass spectrometry (CLMS) holds promise to identify interaction sites in larger and more complex biological systems. The typical CLMS workflow allows for the measurement of the proximity in three-dimensional space of amino acids, identifying proteins in direct contact with DNA or RNA, and it provides information on the folds of proteins as well as their topology in the complexes. Principal CLMS applications, its notable successes, as well as common pipelines that bridge proteomics, molecular biology, structural systems biology, and interactomics are outlined.
Subject(s)
Key words

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Mass Spectrometry / Proteins Limits: Animals / Humans Language: En Journal: Biomolecules Year: 2021 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Mass Spectrometry / Proteins Limits: Animals / Humans Language: En Journal: Biomolecules Year: 2021 Document type: Article Affiliation country:
...