Composition and charge state influence on the ion-neutral collision cross sections of protonated N-linked glycopeptides: an experimental and theoretical deconstruction of coulombic repulsion vs. charge solvation effects.

Ion mobility spectrometry (IMS) is of significant interest as a platform for glycoanalysis. While much attention has been focused on the resolution of isomeric carbohydrates and glycoconjugates, another appealing aspect of IMS is the ability to sort different classes of biomolecules into distinct regions of mass vs. mobility space.

A study of calibrant selection in measurement of carbohydrate and peptide ion-neutral collision cross sections by traveling wave ion mobility spectrometry.

While ion-neutral collision cross sections (CCSs) can be directly calculated from drift tube ion mobility spectrometry (DTIMS) data, measurements made using the more recently introduced traveling wave ion mobility spectrometry (TWIMS) technique are usually calibrated using standards with known CCS. Presently, there remains some question regarding how selection of calibrants influences TWIMS CCS measurements. This is of particular concern when calibrants of the same molecular class (e.