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. 1996 Apr 2;93(7):3143-8.
doi: 10.1073/pnas.93.7.3143.

Conformations and folding of lysozyme ions in vacuo

D S Gross  1 , P D Schnier, S E Rodriguez-Cruz, C K Fagerquist, E R Williams
Affiliations

Conformations and folding of lysozyme ions in vacuo

D S Gross et al. Proc Natl Acad Sci U S A. .

Abstract

Proton transfer reactivity of isolated charge states of the protein hen egg-white lysozyme shows that multiple distinct conformations of this protein are stable in the gas phase. The reactivities of the 9+ and 10+ charge state ions, formed by electrospray ionization of "native" (disulfide-intact) and "denatured" (disulfide-reduced) solutions, are consistent with values calculated for ions in their crystal structure and fully denatured conformations, respectively. Charge states below 8+ of both forms, formed by proton stripping, have similar or indistinguishable reactivities, indicating that the disulfide-reduced ions fold in the gas phase to a more compact conformation.

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