scholarly journals Binding of dihydroxybenzenes in a synthetic molecular clip. Effect of hydrogen bonding and .pi.-stacking

1991 ◽  
Vol 56 (10) ◽  
pp. 3199-3201 ◽  
Author(s):  
Rint P. Sijbesma ◽  
Arno P. M. Kentgens ◽  
Roeland J. M. Nolte

2020 ◽  
Vol 44 (14) ◽  
pp. 5410-5418 ◽  
Author(s):  
Sunshine Dominic Kurbah ◽  
Ram A. Lal

We report the synthesis and characterization of a new self-assembled VO2-L metallogel. Multi-responsive properties of the gel were also studied and can be used for sensing OH− anions. Bromoperoxidase-like activity of VO2-L metallogel for oxidative bromination reaction was also reported.



2016 ◽  
Vol 18 (30) ◽  
pp. 20189-20198 ◽  
Author(s):  
Quynh L. Nguyen ◽  
Vincent A. Spata ◽  
Spiridoula Matsika

The fluorescence properties of pyrrolocytosine, a cytosine analogue, are investigated using high level ab initio methods, and they are found to be affected by hydrogen bonding to water molecules, as well as by pi-stacking with guanine.



2021 ◽  
Vol 22 (3) ◽  
pp. 1335
Author(s):  
Kristen Scopino ◽  
Carol Dalgarno ◽  
Clara Nachmanoff ◽  
Daniel Krizanc ◽  
Kelly M. Thayer ◽  
...  

The ribosome CAR interaction surface is hypothesized to provide a layer of translation regulation through hydrogen-bonding to the +1 mRNA codon that is next to enter the ribosome A site during translocation. The CAR surface consists of three residues, 16S/18S rRNA C1054, A1196 (E. coli 16S numbering), and R146 of yeast ribosomal protein Rps3. R146 can be methylated by the Sfm1 methyltransferase which is downregulated in stressed cells. Through molecular dynamics analysis, we show here that methylation of R146 compromises the integrity of CAR by reducing the cation-pi stacking of the R146 guanidinium group with A1196, leading to reduced CAR hydrogen-bonding with the +1 codon. We propose that ribosomes assembled under stressed conditions have unmethylated R146, resulting in elevated CAR/+1 codon interactions, which tunes translation levels in response to the altered cellular context.



2019 ◽  
Vol 7 (2) ◽  
pp. 39-46
Author(s):  
Rahul Kumar Ancheria ◽  
Saloni Jain ◽  
Deepak Kumar ◽  
Sankar Lal Soni ◽  
Mukesh Sharma

Pharmaceutical co-crystals are nonionic supramolecular complexes and supramolecular chemistry. Pharmaceutical co-crystal consists of active pharmaceutical ingredients and coformers. Pharmaceutical co-crystals can be employed to improve vital physicochemical characteristics of a drug, including solubility, dissolution, bioavailability and stability of pharmaceutical compounds while maintaining its therapeutic activity. Co-crystals can be constructed through several types of interaction, including hydrogen bonding, pi-stacking, and vander Waals forces. Pharmaceutical co-crystals could play a major role in the future of API formulation. Pharmaceutical co-crystal can be improvement future aspect problems related physicochemical properties of API



2020 ◽  
Author(s):  
Kristen Scopino ◽  
Carol Dalgarno ◽  
Clara Nachmanoff ◽  
Daniel Krizanc ◽  
Kelly M. Thayer ◽  
...  

AbstractThe ribosome CAR interaction surface is hypothesized to provide a layer of translation regulation through hydrogen-bonding to the +1 mRNA codon that is next to enter the ribosome A site during translocation. The CAR surface consists of three residues, 16S/18S rRNA C1054, A1196 (E. coli 16S numbering), and R146 of yeast ribosomal protein Rps3. R146 can be methylated by the Sfm1 methyltransferase which is downregulated in stressed cells. Through molecular dynamics analysis, we show here that methylation of R146 compromises the integrity of CAR by reducing the pi stacking of the R146 guanidinium group with A1196, leading to reduced CAR hydrogen-bonding with the +1 codon. We propose that ribosomes assembled under stressed conditions have unmethylated R146, resulting in elevated CAR/+1 codon interactions, which tunes translation levels in response to the altered cellular context.



2000 ◽  
Vol 98 (3) ◽  
pp. 125-134 ◽  
Author(s):  
T. Weitkamp, J. Neuefeind, H. E. Fisch


Sign in / Sign up

Export Citation Format

Share Document