Effect of metal ion binding on the secondary structure of bovine .alpha.-lactalbumin as examined by infrared spectroscopy

Biochemistry ◽  
1991 ◽  
Vol 30 (36) ◽  
pp. 8797-8804 ◽  
Author(s):  
Steven J. Prestrelski ◽  
D. Michael Byler ◽  
Marvin P. Thompson
Keyword(s):  
Infrared Spectroscopy ◽  
Secondary Structure ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Alpha Lactalbumin

Interaction of RNase A with VO3-and VO2+Ions. Metal Ion Binding Mode and Protein Secondary Structure

1999 ◽  
Vol 17 (3) ◽  
pp. 473-480 ◽  
Author(s):  
M. Purcell ◽  
A. Novetta-Delen ◽  
H. Arakawa ◽  
H. Malonga ◽  
H. A. Tajmir-Riahi
Keyword(s):  
Secondary Structure ◽  
Metal Ion ◽  
Protein Secondary Structure ◽  
Binding Mode ◽  
Rnase A ◽  
Ion Binding ◽  
Metal Ion Binding

Metal ion binding to .alpha.-lactalbumin species

Biochemistry ◽  
1982 ◽  
Vol 21 (22) ◽  
pp. 5488-5494 ◽  
Author(s):  
Kentaro Murakami ◽  
Piet Jan Andree ◽  
Lawrence J. Berliner
Keyword(s):  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Alpha Lactalbumin

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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