Infrared Spectroscopy of Water Cluster Anions, (H2O)n=3-24- in the HOH Bending Region: Persistence of the Double H-Bond Acceptor (AA) Water Molecule in the Excess Electron Binding Site of the Class I Isomers.

ChemInform ◽  
2006 ◽  
Vol 37 (35) ◽  
Author(s):  
Joseph R. Roscioli ◽  
Nathan I. Hammer ◽  
M. A. Johnson
Keyword(s):  
Infrared Spectroscopy ◽  
Water Molecule ◽  
Binding Site ◽  
Water Cluster ◽  
Excess Electron ◽  
Class I ◽  
Cluster Anions ◽  
Electron Binding

scholarly journals Importance of self-interaction-error removal in density functional calculations on water cluster anions

2020 ◽  
Vol 22 (7) ◽  
pp. 3789-3799 ◽  
Author(s):  
Jorge Vargas ◽  
Peter Ufondu ◽  
Tunna Baruah ◽  
Yoh Yamamoto ◽  
Koblar A. Jackson ◽  
...  
Keyword(s):  
Density Functional Calculations ◽  
Water Cluster ◽  
Density Functional ◽  
Binding Energies ◽  
Cluster Anions ◽  
Orbital Energies ◽  
Error Removal ◽  
Electron Binding Energies ◽  
Electron Binding

Removing self-interaction errors in density functional approximations results in significantly improved vertical detachment energies of water anions and is essential for obtaining orbital energies consistent with electron binding energies.

scholarly journals Interior- and surface-bound excess electron states in large water cluster anions

2009 ◽  
Vol 130 (12) ◽  
pp. 124319 ◽  
Author(s):  
Ádám Madarász ◽  
Peter J. Rossky ◽  
László Turi
Keyword(s):  
Water Cluster ◽  
Excess Electron ◽  
Cluster Anions ◽  
Electron States ◽  
Large Water

scholarly journals Inhibitory mechanism of reveromycin A at the tRNA binding site of a class I synthetase

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Bingyi Chen ◽  
Siting Luo ◽  
Songxuan Zhang ◽  
Yingchen Ju ◽  
Qiong Gu ◽  
...  
Keyword(s):  
Binding Site ◽  
Catalytic Domain ◽  
Trna Synthetase ◽  
Rational Drug Design ◽  
Class I ◽  
Binding Assays ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Rational Drug ◽  
Trna Binding

AbstractThe polyketide natural product reveromycin A (RM-A) exhibits antifungal, anticancer, anti-bone metastasis, anti-periodontitis and anti-osteoporosis activities by selectively inhibiting eukaryotic cytoplasmic isoleucyl-tRNA synthetase (IleRS). Herein, a co-crystal structure suggests that the RM-A molecule occupies the substrate tRNAIle binding site of Saccharomyces cerevisiae IleRS (ScIleRS), by partially mimicking the binding of tRNAIle. RM-A binding is facilitated by the copurified intermediate product isoleucyl-adenylate (Ile-AMP). The binding assays confirm that RM-A competes with tRNAIle while binding synergistically with l-isoleucine or intermediate analogue Ile-AMS to the aminoacylation pocket of ScIleRS. This study highlights that the vast tRNA binding site of the Rossmann-fold catalytic domain of class I aminoacyl-tRNA synthetases could be targeted by a small molecule. This finding will inform future rational drug design.

scholarly journals Ion-Dependent Binding-Site Configurations in Ef-Hand Proteins Measured with Ultrafast Infrared Spectroscopy

2019 ◽  
Vol 116 (3) ◽  
pp. 49a
Author(s):  
Sean Edington ◽  
Thomas R. Middendorf ◽  
David Brent Halling ◽  
Richard W. Aldrich ◽  
Carlos R. Baiz
Keyword(s):  
Infrared Spectroscopy ◽  
Binding Site ◽  
Ef Hand ◽  
Ultrafast Infrared
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