scholarly journals Effects of conformational ordering on protein/polyelectrolyte electrostatic complexation: ionic binding and chain stiffening

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Yiping Cao ◽  
Yapeng Fang ◽  
Katsuyoshi Nishinari ◽  
Glyn O. Phillips
Keyword(s):  
Conformational Ordering ◽  
Ionic Binding

scholarly journals Encapsulation of Risperidone into Chitosan-based Nanocarrier via Ionic Binding Interaction

2014 ◽  
Vol 13 ◽  
pp. 92-100 ◽  
Author(s):  
Diky Mudhakir ◽  
Caroline Wibisono ◽  
Heni Rachmawati
Keyword(s):  
Binding Interaction ◽  
Ionic Binding

scholarly journals The Electrostatic Basis of Diacylglycerol Pyrophosphate—Protein Interaction

Cells ◽  
2022 ◽  
Vol 11 (2) ◽  
pp. 290
Author(s):  
Zachary Graber ◽  
Desmond Owusu Kwarteng ◽  
Shannon M. Lange ◽  
Yannis Koukanas ◽  
Hady Khalifa ◽  
...  
Keyword(s):  
Phosphatidic Acid ◽  
Protein Interaction ◽  
Anionic Phospholipid ◽  
Tryptophan Residues ◽  
Switch Mechanism ◽  
31P Mas Nmr ◽  
Calcium And Magnesium ◽  
Ionic Binding ◽  
Novel Model ◽  
Positively Charged

Diacylglycerol pyrophosphate (DGPP) is an anionic phospholipid formed in plants, yeast, and parasites under multiple stress stimuli. It is synthesized by the phosphorylation action of phosphatidic acid (PA) kinase on phosphatidic acid, a signaling lipid with multifunctional properties. PA functions in the membrane through the interaction of its negatively charged phosphomonoester headgroup with positively charged proteins and ions. DGPP, like PA, can interact electrostatically via the electrostatic-hydrogen bond switch mechanism but differs from PA in its overall charge and shape. The formation of DGPP from PA alters the physicochemical properties as well as the structural dynamics of the membrane. This potentially impacts the molecular and ionic binding of cationic proteins and ions with the DGPP enriched membrane. However, the results of these important interactions in the stress response and in DGPP’s overall intracellular function is unknown. Here, using 31P MAS NMR, we analyze the effect of the interaction of low DGPP concentrations in model membranes with the peptides KALP23 and WALP23, which are flanked by positively charged Lysine and neutral Tryptophan residues, respectively. Our results show a significant effect of KALP23 on the charge of DGPP as compared to WALP23. There was, however, no significant effect on the charge of the phosphomonoester of DGPP due to the interaction with positively charged lipids, dioleoyl trimethylammonium propane (DOTAP) and dioleoyl ethyl-phosphatidylcholine (EtPC). Divalent calcium and magnesium cations induce deprotonation of the DGPP headgroup but showed no noticeable differences on DGPP’s charge. Our results lead to a novel model for DGPP—protein interaction.

On features of the conformational ordering of natural and synthetic cis-1,4-polyisoprenes

1985 ◽  
Vol 27 (7) ◽  
pp. 1652-1660 ◽  
Author(s):  
K.V Nel'son ◽  
A.P Berezkina ◽  
S.K Kurlyand
Keyword(s):  
Conformational Ordering ◽  
Natural And Synthetic

Shear-Induced Conformational Ordering, Relaxation, and Crystallization of Isotactic Polypropylene

2008 ◽  
Vol 112 (39) ◽  
pp. 12256-12262 ◽  
Author(s):  
Haining An ◽  
Xiangyang Li ◽  
Yong Geng ◽  
Yunlong Wang ◽  
Xiao Wang ◽  
...  
Keyword(s):  
Isotactic Polypropylene ◽  
Conformational Ordering
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