Impacts of polyatomic ions on surfaces: conformation and degree of fragmentation of molecular ions determined by lateral dimensions of impact features

Reimann, C.T.; Quist, Arjan P.; Kopniczky, Judit; Sundqvist, B.; Erlandsson, R.; Tengvall, Pentti

doi:10.1016/0168-583x(94)96076-3

Cited by 29 publications

(25 citation statements)

References 13 publications

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“…In a previous work of ours/ tentative results were reported on similar impact experiments performed with native and disulfide-reduced albumin [26]. Impact hillocks formed with electrosprayed native albumin were somewhat elongated, consistent with partial Coulombic-driven denaturation of this three-domain blood protein [44].…”

Section: Conformation Of Lys 10 +supporting

confidence: 77%

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Defect formation on surfaces bombarded by energetic multiply charged proteins: Implications for the conformation of gas-phase electrosprayed ions

Sullivan

Axelsson

Altmann

et al. 1996

J. Am. Soc. Mass Spectrom.

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Indirect information on the conformation of highly charged molecular ions may be obtained by monitoring their collisional cross sections and the course of simple gas-phase reactions such as hydrogen-deuterium exchange. In this work, another indirect but more visually oriented approach is explored: electrosprayed protein ions are accelerated toward a highly oriented pyrolytic graphite surface and the resulting single-ion defects are imaged by scanning force and tunneling microscopy. All protein impacts generated shallow hillocks: the shapes depended on the identity and charge state of the incident protein. Lysozyme and myoglobin, both compact, globular proteins in the native state, produced compact, almost circular hillocks. However, hillocks generated by myoglobin that had been denatured in the solution phase were elongated, and the elongation was positively correlated with the charge state of the ion. It appears that structural information about gas-phase multiply charged proteins can be derived from imprints generated by energetic protein impacts on surfaces.

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Section: Conformation Of Lys 10 +supporting

confidence: 77%

“…Energetic protein ions were generated by using the multiply charged macromolecular accelerator (MUMMA) at Uppsala. This apparatus has been described in detail elsewhere ( [21][22][23][24][25][26][27][28] and Hakansson, P.;…”

Section: Methodsmentioning

confidence: 99%

Defect formation on surfaces bombarded by energetic multiply charged proteins: Implications for the conformation of gas-phase electrosprayed ions

Sullivan

Axelsson

Altmann

et al. 1996

J. Am. Soc. Mass Spectrom.

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“…In the hopes of providing further complementary information on the detailed structure of gas-phase bio-molecular ions, Reimann and co-workers [100] have exploited a visually oriented approach. Using the "multiply charged macromolecular accelerator" (MUMMA), protein ions Energy diffusion and surface modification lead to a broadening of the surface defects.…”

Section: Energetic Surface Imprintingmentioning

confidence: 99%

“…In the first study of biomolecular ions using this method, Reimann and co-workers [100] examined the +41 charge state of disulfide-intact and +47 charge state of disulfide-reduced bovine albumin. The elliptical defects observed for the disulfide-intact ions were larger than would be expected if albumin retained its native shape; the expansion of these ions was attributed to Coulombic repulsion.…”

Section: Energetic Surface Imprintingmentioning

confidence: 99%

Collision cross sections of gas phase DNA ions

Moradian

Scalf

Westphall

et al. 2002

International Journal of Mass Spectrometry

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In presenting this thesis in partial fulfilment of the requirements for an advanced degree at the University of British Columbia, I agree that the Library shall make it freely available for reference and study. 1 further agree that permission for extensive copying of this thesis for scholarly purposes may be granted by the head of my department or by his or her representatives. It is understood that copying or publication of this thesis for financial gain shall not be allowed without my written permission.

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“…A special new technique has been applied to study the shape of large molecules in the gas phase (199). Massive, multiply charged ions formed by ES have been directed towards a flat target surface.…”

Section: Peptide and Protein Conformationsmentioning

confidence: 99%

Multiply charged ions

Vékey¹

1995

Mass Spectrometry Reviews

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Formation, characteristics of, and applications using doubly and multiply charged ions are reviewed in the present article. The main emphasis is on medium‐ to large‐sized molecules, from the point‐of‐view of organic, physico‐organic, and bio‐organic mass spectrometry. Multiply charged species can be studied by all conventional mass spectrometric techniques. Those techniques and reaction types that are particularly relevant to multiply charged ions are discussed in some detail in Section III. Studies on small‐ to medium‐sized molecules are discussed in Section IV. A particularly interesting aspect, the distinction of doubly charged isomeric ions, is also treated here. Multiply charged ions of large (bio‐)molecules are discussed in Section V. This area is fast expanding, mainly due to the spread of electrospray ionization. Fragmentation and conformation of multiply protonated peptides is discussed in detail. © 1996 John Wiley & Sons, Inc.

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Impacts of polyatomic ions on surfaces: conformation and degree of fragmentation of molecular ions determined by lateral dimensions of impact features

Cited by 29 publications

References 13 publications

Defect formation on surfaces bombarded by energetic multiply charged proteins: Implications for the conformation of gas-phase electrosprayed ions

Defect formation on surfaces bombarded by energetic multiply charged proteins: Implications for the conformation of gas-phase electrosprayed ions

Collision cross sections of gas phase DNA ions

Multiply charged ions

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