scholarly journals Characterization of gas phase aggregates of bis(2-ethylhexyl)sulfosuccinate (AOT) and divalent metal ions. Elimination of radical species in the decomposition pathways of even-electron [AOTMIICl2]-anions

2012 ◽  
Vol 47 (12) ◽  
pp. 1537-1545 ◽  
Author(s):  
Gianluca Giorgi ◽  
Leopoldo Ceraulo ◽  
Vincenzo Turco Liveri
Keyword(s):  
Metal Ions ◽  
Gas Phase ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Radical Species

Synthesis and characterization of bis(imino)pyridine complexes of divalent Mg and Zn

2016 ◽  
Vol 45 (14) ◽  
pp. 5989-5998 ◽  
Author(s):  
Thomas W. Myers ◽  
Tobias J. Sherbow ◽  
James C. Fettinger ◽  
Louise A. Berben
Keyword(s):  
Electronic Structure ◽  
Metal Ions ◽  
Torsion Angle ◽  
Divalent Metal ◽  
Synthesis And Characterization ◽  
Divalent Metal Ions ◽  
Structural Comparison ◽  
Bond Lengths ◽  
Pyridine Complexes

The synthesis and electronic structure of bis(imino)pyridine (I2P) complexes of the divalent metal ions, Zn(ii) and Mg(ii) are reported, and a correlation between the ligand Cim–Cpy bond lengths with the ligand torsion angle is described. Structural comparison with a new complex of Al(iii) and previously reported Al(iii) complexes is included.

scholarly journals Binding of Divalent Metal Ions with Deprotonated Peptides: Do Gas-Phase Anions Parallel the Condensed Phase?

2018 ◽  
Vol 122 (25) ◽  
pp. 5589-5596 ◽  
Author(s):  
Robert C. Dunbar ◽  
Jonathan Martens ◽  
Giel Berden ◽  
Jos Oomens
Keyword(s):  
Metal Ions ◽  
Gas Phase ◽  
Condensed Phase ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Deprotonated Peptides

scholarly journals Exploring the underwater silken architectures of caddisworms: comparative silkomics across two caddisfly suborders

2019 ◽  
Vol 374 (1784) ◽  
pp. 20190206 ◽  
Author(s):  
Paul B. Frandsen ◽  
Madeline G. Bursell ◽  
Adam M. Taylor ◽  
Seth B. Wilson ◽  
Amy Steeneck ◽  
...  
Keyword(s):  
Metal Ions ◽  
Silk Gland ◽  
Divalent Metal ◽  
Aqueous Environment ◽  
Silk Fibre ◽  
Divalent Metal Ions ◽  
Molar Ratios ◽  
Initial Characterization ◽  
Underwater Structures

Caddisfly (Trichoptera) larvae assemble a variety of underwater structures using bioadhesive silk. The order is divided into two primary sub-orders distinguished by how the larvae deploy their silk. Foraging Integripalpia larvae construct portable tube cases. Annulipalpia larvae construct stationary retreats, some with suspended nets to capture food. To identify silk molecular adaptations that may have contributed to caddisfly diversification, we report initial characterization of silk from a net-spinner genus, Parapsyche, for comparison with the silk of a tube case-maker genus, Hesperophylax . Overall, general features of silk structure and processing are conserved across the sub-orders despite approximately 200 Ma of divergence: the H-fibroin proteins comprise repeating phosphoserine-rich motifs, naturally spun silk fibres contain approximately 1 : 1 molar ratios of divalent metal ions to phosphate, silk fibre precursors are stored as complex fluids of at least two types of complexes, and silk gland proteins contain only traces of divalent metal ions, suggesting metal ions that solidify the fibres are absorbed from the aqueous environment after silk extrusion. However, the number and arrangement of the repeating phosphoserine blocks differ between genera, suggesting molecular adaptation of H-fibroin through duplication and shuffling of conserved structural modules may correspond with the radiation of caddisflies into diverse environments. This article is part of the theme issue ‘Transdisciplinary approaches to the study of adhesion and adhesives in biological systems’.

scholarly journals NMR Characterization of the Interaction of the Endonuclease Domain of MutL with Divalent Metal Ions and ATP

PLoS ONE ◽  
2014 ◽  
Vol 9 (6) ◽  
pp. e98554 ◽  
Author(s):  
Ryota Mizushima ◽  
Ju Yaen Kim ◽  
Isao Suetake ◽  
Hiroaki Tanaka ◽  
Tomoyo Takai ◽  
...  
Keyword(s):  
Metal Ions ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Nmr Characterization ◽  
Endonuclease Domain
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