Conformations and folding of lysozyme ions in vacuo.
收藏PubMed Central1996-04-02 更新2026-05-02 收录
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https://pmc.ncbi.nlm.nih.gov/articles/PMC39776/
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资源简介：
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. IMAGES:
提供机构：
National Academy of Sciences
创建时间：
1996-04-02
