Development of large-scale cross-linking mass spectrometry
Barysz, Helena Maria LU and Malmstroem, Johan LU
(2018)
In Molecular and Cellular Proteomics
17(6).
p.1055-1066
- Abstract
Cross-linking mass spectrometry (CLMS) provides distance constraints to study the structure of proteins, multiprotein complexes and protein-protein interactions which are critical for the understanding of protein function. CLMS is an attractive technology to bridge the gap between high-resolution structural biology techniques and proteomic-based interactome studies. However, as outlined in this review there are still several bottlenecks associated with CLMS which limit its application on a proteome-wide level. Specifically, there is an unmet need for comprehensive software that can reliably identify cross-linked peptides from large datasets. In this review we provide supporting information to reason that targeted proteomics of... (More)
Cross-linking mass spectrometry (CLMS) provides distance constraints to study the structure of proteins, multiprotein complexes and protein-protein interactions which are critical for the understanding of protein function. CLMS is an attractive technology to bridge the gap between high-resolution structural biology techniques and proteomic-based interactome studies. However, as outlined in this review there are still several bottlenecks associated with CLMS which limit its application on a proteome-wide level. Specifically, there is an unmet need for comprehensive software that can reliably identify cross-linked peptides from large datasets. In this review we provide supporting information to reason that targeted proteomics of cross-links may provide the required sensitivity to reliably detect and quantify cross-linked peptides and that a reporter ion signature for cross-linked peptides may become a useful approach to increase confidence in the identification process of cross-linked peptides. In addition, the review summarizes the recent advances in CLMS workflows using the analysis of condensin complex in intact chromosomes as a model complex.
(Less)
- author
- Barysz, Helena Maria
LU
and Malmstroem, Johan
LU
- organization
- publishing date
- 2018
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular and Cellular Proteomics
- volume
- 17
- issue
- 6
- pages
- 1055 - 1066
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:28389583
- scopus:85023172595
- ISSN
- 1535-9484
- DOI
- 10.1074/mcp.R116.061663
- language
- English
- LU publication?
- yes
- id
- 1863652d-a7b2-455b-865f-da33444d36c1
- date added to LUP
- 2017-09-04 17:26:37
- date last changed
- 2025-10-14 11:21:59
@article{1863652d-a7b2-455b-865f-da33444d36c1,
abstract = {{<p>Cross-linking mass spectrometry (CLMS) provides distance constraints to study the structure of proteins, multiprotein complexes and protein-protein interactions which are critical for the understanding of protein function. CLMS is an attractive technology to bridge the gap between high-resolution structural biology techniques and proteomic-based interactome studies. However, as outlined in this review there are still several bottlenecks associated with CLMS which limit its application on a proteome-wide level. Specifically, there is an unmet need for comprehensive software that can reliably identify cross-linked peptides from large datasets. In this review we provide supporting information to reason that targeted proteomics of cross-links may provide the required sensitivity to reliably detect and quantify cross-linked peptides and that a reporter ion signature for cross-linked peptides may become a useful approach to increase confidence in the identification process of cross-linked peptides. In addition, the review summarizes the recent advances in CLMS workflows using the analysis of condensin complex in intact chromosomes as a model complex.</p>}},
author = {{Barysz, Helena Maria and Malmstroem, Johan}},
issn = {{1535-9484}},
language = {{eng}},
number = {{6}},
pages = {{1055--1066}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Molecular and Cellular Proteomics}},
title = {{Development of large-scale cross-linking mass spectrometry}},
url = {{http://dx.doi.org/10.1074/mcp.R116.061663}},
doi = {{10.1074/mcp.R116.061663}},
volume = {{17}},
year = {{2018}},
}