Cheetah-MS: A web server to model protein complexes using tandem cross-linking mass spectrometry data

Summary: Protein-protein interactions (PPIs) are central in many biological processes but difficult to characterize, especially in complex, unfractionated samples. Chemical cross-linking combined with mass spectrometry (MS) and computational modeling is gaining recognition as a viable tool in protei...

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Bibliographic Details
Main Authors: Happonen, L. (Author), Khakzad, H. (Author), Malmström, J. (Author), Malmström, L. (Author)
Format: Article
Language:English
Published: Oxford University Press 2021
Online Access:View Fulltext in Publisher
LEADER 01469nam a2200169Ia 4500
001 10.1093-bioinformatics-btab449
008 220427s2021 CNT 000 0 und d
020 |a 13674803 (ISSN) 
245 1 0 |a Cheetah-MS: A web server to model protein complexes using tandem cross-linking mass spectrometry data 
260 0 |b Oxford University Press  |c 2021 
856 |z View Fulltext in Publisher  |u https://doi.org/10.1093/bioinformatics/btab449 
520 3 |a Summary: Protein-protein interactions (PPIs) are central in many biological processes but difficult to characterize, especially in complex, unfractionated samples. Chemical cross-linking combined with mass spectrometry (MS) and computational modeling is gaining recognition as a viable tool in protein interaction studies. Here, we introduce Cheetah-MS, a web server for predicting the PPIs in a complex mixture of samples. It combines the capability and sensitivity of MS to analyze complex samples with the power and resolution of protein-protein docking. It produces the quaternary structure of the PPI of interest by analyzing tandem MS/MS data (also called MS2). Combining MS analysis and modeling increases the sensitivity and, importantly, facilitates the interpretation of the results. © 2021 The Author(s) 2021. Published by Oxford University Press. 
700 1 |a Happonen, L.  |e author 
700 1 |a Khakzad, H.  |e author 
700 1 |a Malmström, J.  |e author 
700 1 |a Malmström, L.  |e author 
773 |t Bioinformatics