Conformations and folding of lysozyme ions in vacuo.
basic_science · Level V
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- Record sourced from PubMed, PMID 8610183.
- Also identified by PMC identifier 39776.
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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.
Medical subject headings
- Muramidase
- Protein Conformation
- Protein Folding