scholarly journals Broad, intense, quiescent beam of singly charged metal ions obtained by extraction from self-sputtering plasma far above the runaway threshold

2009 ◽  
Vol 106 (2) ◽  
pp. 023306 ◽  
Author(s):  
André Anders ◽  
Efim Oks
Keyword(s):  
Metal Ions ◽  
Singly Charged ◽  
Charged Metal Ions

Electron-impact excitation of singly charged metal ions

2011 ◽  
Vol 83 (6) ◽  
Author(s):  
L. Sharma ◽  
A. Surzhykov ◽  
R. Srivastava ◽  
S. Fritzsche
Keyword(s):  
Metal Ions ◽  
Electron Impact ◽  
Impact Excitation ◽  
Electron Impact Excitation ◽  
Singly Charged ◽  
Charged Metal Ions

scholarly journals Metal ions shape α-synuclein

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Rani Moons ◽  
Albert Konijnenberg ◽  
Carl Mensch ◽  
Roos Van Elzen ◽  
Christian Johannessen ◽  
...  
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Specific Binding ◽  
Intrinsically Disordered Protein ◽  
Cellular Interactions ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Conformational Effects ◽  
Complex Structural ◽  
Singly Charged

Abstract α-Synuclein is an intrinsically disordered protein that can self-aggregate and plays a major role in Parkinson’s disease (PD). Elevated levels of certain metal ions are found in protein aggregates in neurons of people suffering from PD, and environmental exposure has also been linked with neurodegeneration. Importantly, cellular interactions with metal ions, particularly Ca2+, have recently been reported as key for α-synuclein’s physiological function at the pre-synapse. Here we study effects of metal ion interaction with α-synuclein at the molecular level, observing changes in the conformational behaviour of monomers, with a possible link to aggregation pathways and toxicity. Using native nano-electrospray ionisation ion mobility-mass spectrometry (nESI-IM-MS), we characterize the heterogeneous interactions of alkali, alkaline earth, transition and other metal ions and their global structural effects on α-synuclein. Different binding stoichiometries found upon titration with metal ions correlate with their specific binding affinity and capacity. Subtle conformational effects seen for singly charged metals differ profoundly from binding of multiply charged ions, often leading to overall compaction of the protein depending on the preferred binding sites. This study illustrates specific effects of metal coordination, and the associated electrostatic charge patterns, on the complex structural space of the intrinsically disordered protein α-synuclein.

Production of Highly Charged Metal Ions and Soft X-Ray Emission in a Plasma Focus

1988 ◽  
Vol 27 (Part 1, No. 1) ◽  
pp. 89-94 ◽  
Author(s):  
Katsumi Hirano ◽  
Toshikazu Yamamoto ◽  
Satoshi Takada ◽  
Hisao Sone ◽  
Katsuji Shimada
Keyword(s):  
Metal Ions ◽  
Plasma Focus ◽  
X Ray ◽  
Charged Metal Ions

Multiply charged metal ions in high current pulsed vacuum arcs

2017 ◽  
Vol 24 (12) ◽  
pp. 123501 ◽  
Author(s):  
G. Yu. Yushkov ◽  
A. G. Nikolaev ◽  
V. P. Frolova ◽  
E. M. Oks ◽  
A. G. Rousskikh ◽  
...  
Keyword(s):  
Metal Ions ◽  
High Current ◽  
Multiply Charged ◽  
Charged Metal Ions

Hydration of some large and highly charged metal ions

2001 ◽  
Vol 8 (2) ◽  
pp. 657-659 ◽  
Author(s):  
Magnus Sandström ◽  
Ingmar Persson ◽  
Farideh Jalilehvand ◽  
Patric Lindquist-Reis ◽  
Daniel Spångberg ◽  
...  
Keyword(s):  
Metal Ions ◽  
Charged Metal Ions
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