Analysis of Protein-Glycosaminoglycan Interactions Using Traveling Wave Ion-Mobility Mass Spectrometry
Overview
Overview
Authors
Authors
Affiliations
Affiliations
Soon will be listed here.
Abstract
Traveling wave ion-mobility mass spectrometry (TWIMS) combined with native mass spectrometry (MS) has emerged as a powerful tool for analyzing biomolecules, including complexes of protein and heparan sulfate (HS). This technique allows determination of the stoichiometry of the protein-HS interaction and information on the overall 3D molecular envelope.
References
1.
Hernandez H, Robinson C
. Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry. Nat Protoc. 2007; 2(3):715-26.
DOI: 10.1038/nprot.2007.73.
View
2.
Benesch J, Ruotolo B
. Mass spectrometry: come of age for structural and dynamical biology. Curr Opin Struct Biol. 2011; 21(5):641-9.
PMC: 3193349.
DOI: 10.1016/j.sbi.2011.08.002.
View
3.
Zhao Y, Singh A, Li L, Linhardt R, Xu Y, Liu J
. Investigating changes in the gas-phase conformation of Antithrombin III upon binding of Arixtra using traveling wave ion mobility spectrometry (TWIMS). Analyst. 2015; 140(20):6980-9.
PMC: 4586392.
DOI: 10.1039/c5an00908a.
View
4.
Zhao Y, Singh A, Xu Y, Zong C, Zhang F, Boons G
. Gas-Phase Analysis of the Complex of Fibroblast GrowthFactor 1 with Heparan Sulfate: A Traveling Wave Ion Mobility Spectrometry (TWIMS) and Molecular Modeling Study. J Am Soc Mass Spectrom. 2016; 28(1):96-109.
PMC: 5177502.
DOI: 10.1007/s13361-016-1496-8.
View
5.
Ruotolo B, Benesch J, Sandercock A, Hyung S, Robinson C
. Ion mobility-mass spectrometry analysis of large protein complexes. Nat Protoc. 2008; 3(7):1139-52.
DOI: 10.1038/nprot.2008.78.
View