Capillary and Coulombic effects on the gas phase structure of electrosprayed concanavalin A ions and its clusters C(n)(+z) (n = 1-6).

Ion mobility spectrometry (IMS) coupled to mass spectrometry (MS) is used to study the gas phase collision cross section Ω(z, n) in CO(2) of multimers C(n) (n = 1-4, 6) of concanavalin A, whose tetramer C(4) has a crystal structure resembling four tetrahedrically arranged globules. C(n)(+z) ions electrosprayed from aqueous solutions of triethylammonium formate (Et(3)AF) are moderately charged (up to z = 6 and 17 for n = 1 and 6) and produce narrow mobility peaks. Charge states down to z = 1 obtained with a charge-reducing radioactive (63)Ni source are studied for the dimer and the tetramer via pure IMS (no MS). The mobilities are independent of pH in the range 6-8, controlled by addition of triethylamine to the Et(3)AF. The measured compactness group Ω(z, n)/n(2/3) is practically independent of n and z, whereas mobility calculations with clusters of touching spheres show that it should vary with n by 20-30% for a variety of scattering models. This contrast suggests that, irrespective of ambiguities on the scattering model, all multimers adopt globular shapes, precluding in particular a tetrahedral tetramer. Acetic acid solutions (87 mM aqueous) yield ions with substantially higher z, mostly with broad mobility distributions. Exceptionally high z tetramers (z = 25-29) and trimers have narrowly defined mobilities with compact but nonspherical shapes. Addition of 2-4 mM Et(3)AF to the 87 mM aqueous acetic acid solution yields narrowly defined mobilities almost identical at all z values to those from the Et(3)AF buffer, although with higher charge states showing also a transition to nonspherical shapes. We conclude that all gas phase clusters charged below a Rayleigh-like charge, z(R), are globular without regard to solution conditions, some undergoing a sharp shape transition at a critical z = z(R). We confirm that gas phase protein cross sections differ from those expected from the crystal structure, with a trend to compact probably driven by their high surface energy (and opposed by Coulombic stresses). The Rayleigh-like shape transitions seen are similar to those arising in linear homopolymers, although not as sharply defined. They yield a surface energy for protein matter almost as high as the surface tension of water. This quantitative conclusion is corroborated by prior data on cytochrome c and apomyoglobin (also showing a critical shape transition) as well as measurements of the maximum charge versus mass in aggregates of dipeptides.