Author(s): Gross DS, Schnier PD, RodriguezCruz SE, Fagerquist CK, Williams ER
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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.
This article was published in Proc Natl Acad Sci U S A
and referenced in Journal of Analytical & Bioanalytical Techniques