Cysteine-based fluorescence “turn-on” sensors for Cu2+ and Ag+

RSC Advances ◽  
2014 ◽  
Vol 4 (99) ◽  
pp. 56539-56542 ◽  
Author(s):  
V. Haridas ◽  
P. P. Praveen Kumar ◽  
Cherumuttathu H. Suresh
Keyword(s):  
Amino Acid ◽  
Computational Methods ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Turn On ◽  
Fluorescence Turn On

Amino acid cysteine was transformed to fluorescent turn-on sensors for Cu+2 and Ag+. The metal ion binding was studied in detail by spectroscopic, microscopic, calorimetric and computational methods.

scholarly journals Identification of metal ion binding sites based on amino acid sequences

PLoS ONE ◽  
2017 ◽  
Vol 12 (8) ◽  
pp. e0183756 ◽  
Author(s):  
Xiaoyong Cao ◽  
Xiuzhen Hu ◽  
Xiaojin Zhang ◽  
Sujuan Gao ◽  
Changjiang Ding ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Sites ◽  
Metal Ion ◽  
Amino Acid Sequences ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Ion Binding Sites ◽  
Metal Ion Binding Sites

Bis-amino Acid Derivatives of 1,1′-Ferrocenedicarboxylic Acid: Structural, Electrochemical, and Metal Ion Binding Studies

2014 ◽  
Vol 33 (18) ◽  
pp. 4873-4887 ◽  
Author(s):  
Bimalendu Adhikari ◽  
Alan J. Lough ◽  
Bryan Barker ◽  
Afzal Shah ◽  
Cuili Xiang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Metal Ion ◽  
Amino Acid Derivatives ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Studies ◽  
Derivatives Of

Photophysical Characterisation, Metal Ion Binding and Enantiomeric Recognition of Chiral Ligands Containing Phenazine Fluorophore

2004 ◽  
Vol 69 (4) ◽  
pp. 885-896 ◽  
Author(s):  
Luisa Stella Dolci ◽  
Péter Huszthy ◽  
Erika Samu ◽  
Marco Montalti ◽  
Luca Prodi ◽  
...  
Keyword(s):  
Metal Ion ◽  
Photophysical Properties ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Ammonium Ions ◽  
Enantiomerically Pure ◽  
Binding Process ◽  
High Affinity ◽  
Enantiomeric Recognition ◽  
Chiral Species

Enantiomerically pure dimethyl- and diisobutyl-substituted phenazino-18-crown-6 ligands bind metal and ammonium ions and also primary aralkylammonium perchlorates in acetonitrile with high affinity, causing pronounced changes in their luminescence properties. In addition, they show enantioselectivity towards chiral primary aralkylammonium perchlorates. The possibility to monitor the binding process by photoluminescence spectroscopy can gain ground for the design of very efficient enantioselective chemosensors for chiral species. The observed changes in the photophysical properties are also an important tool for understanding the interactions present in the adduct.

scholarly journals Snapshots of a Non-Canonical RdRP in Action

Viruses ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1260
Author(s):  
Diego S. Ferrero ◽  
Michela Falqui ◽  
Nuria Verdaguer
Keyword(s):  
Metal Ion ◽  
Rna Viruses ◽  
Ion Binding ◽  
Genome Replication ◽  
Metal Ion Binding ◽  
Insect Virus ◽  
X Ray ◽  
Template Strand ◽  
Nucleotide Incorporation ◽  
Elongation Process

RNA viruses typically encode their own RNA-dependent RNA polymerase (RdRP) to ensure genome replication and transcription. The closed “right hand” architecture of RdRPs encircles seven conserved structural motifs (A to G) that regulate the polymerization activity. The four palm motifs, arranged in the sequential order A to D, are common to all known template dependent polynucleotide polymerases, with motifs A and C containing the catalytic aspartic acid residues. Exceptions to this design have been reported in members of the Permutotetraviridae and Birnaviridae families of positive single stranded (+ss) and double-stranded (ds) RNA viruses, respectively. In these enzymes, motif C is located upstream of motif A, displaying a permuted C–A–B–D connectivity. Here we study the details of the replication elongation process in the non-canonical RdRP of the Thosea asigna virus (TaV), an insect virus from the Permutatetraviridae family. We report the X-ray structures of three replicative complexes of the TaV polymerase obtained with an RNA template-primer in the absence and in the presence of incoming rNTPs. The structures captured different replication events and allowed to define the critical interactions involved in: (i) the positioning of the acceptor base of the template strand, (ii) the positioning of the 3’-OH group of the primer nucleotide during RNA replication and (iii) the recognition and positioning of the incoming nucleotide. Structural comparisons unveiled a closure of the active site on the RNA template-primer binding, before rNTP entry. This conformational rearrangement that also includes the repositioning of the motif A aspartate for the catalytic reaction to take place is maintained on rNTP and metal ion binding and after nucleotide incorporation, before translocation.

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