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- W1978693586 abstract "We present new results from an energetic surface imprinting method which allows us to outline the general conformation of protein ions in vacuo. Both disulfide-bond-intact and disulfide-bond-reduced gas-phase lysozyme ions were produced by electrospray ionization and were accelerated and impacted onto graphite surfaces. The resulting surface defects, each created by a single incident ion, were imaged with scanning force microscopy. Disulfide-intact lysozyme ions created compact, slightly elliptical hillocks on the surfaces, whereas disulfide-reduced lysozyme produced more oblong, elongated hillocks. By employing a thermal model describing the response of graphite to energy deposited by an elongated incident energetic projectile, we calculated from the hillock sizes for disulfide-reduced lysozyme (Q = 14+) an overall length of 32.1 ± 1.6 nm. This value is close to the length we observe for apomyoglobin (Q = 14+), 35.5 ± 2.4 nm, although apomyoglobin and lysozyme possess significantly different numbers of a..." @default.
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- W1978693586 date "1998-07-21" @default.
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- W1978693586 title "Conformation of Highly-Charged Gas-Phase Lysozyme Revealed by Energetic Surface Imprinting" @default.
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- W1978693586 doi "https://doi.org/10.1021/ja980178+" @default.
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