Differential melting voltage by tandem-trapped ion mobility spectrometry: glycan structure influences glycoprotein stability

Abstract

Profiling the full spectrum of protein glycoforms is critical to understanding their functional roles. We developed the differential melting voltage approach using tandem-ion mobility/tandem-mass spectrometry and applied it to study Ribonuclease B glycoforms. Our results indicate that, in addition to glycan mass and intact protein size, the glycan structure plays a role in regulating the stability of Ribonuclease B.

Graphical abstract: Differential melting voltage by tandem-trapped ion mobility spectrometry: glycan structure influences glycoprotein stability

Supplementary files

Article information

Article type
Communication
Submitted
19 May 2025
Accepted
19 Aug 2025
First published
20 Aug 2025
This article is Open Access
Creative Commons BY-NC license

RSC Chem. Biol., 2025, Advance Article

Differential melting voltage by tandem-trapped ion mobility spectrometry: glycan structure influences glycoprotein stability

M. Chai, C. Bleiholder and F. C. Liu, RSC Chem. Biol., 2025, Advance Article , DOI: 10.1039/D5CB00127G

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