scholarly journals Coaction of Electrostatic and Hydrophobic Interactions: Dynamic Constraints on Disordered TrkA Juxtamembrane Domain

2019 ◽  
Vol 123 (50) ◽  
pp. 10709-10717 ◽  
Author(s):  
Zichen Wang ◽  
Huaxun Fan ◽  
Xiao Hu ◽  
John Khamo ◽  
Jiajie Diao ◽  
...  
Keyword(s):  
Hydrophobic Interactions ◽  
Juxtamembrane Domain ◽  
Dynamic Constraints ◽  
Electrostatic And Hydrophobic Interactions

Coaction of Electrostatic and Hydrophobic Interactions: Dynamic Constraints on Disordered TrkA Juxtamembrane Domain

2019 ◽  
Author(s):  
Zichen Wang ◽  
Huaxun Fan ◽  
Xiao Hu ◽  
John Khamo ◽  
Jiajie Diao ◽  
...  
Keyword(s):  
Single Molecule ◽  
Protein Function ◽  
Hydrophobic Interactions ◽  
Transmembrane Helix ◽  
Point Mutations ◽  
Salt Bridge ◽  
Receptor Activation ◽  
Membrane Dynamics ◽  
Juxtamembrane Domain ◽  
Joint Work

<p>The receptor tyrosine kinase family transmits signals into cell via a single transmembrane helix and a flexible juxtamembrane domain (JMD). Membrane dynamics makes it challenging to study the structural mechanism of receptor activation experimentally. In this study, we employ all-atom molecular dynamics with Highly Mobile Membrane-Mimetic to capture membrane interactions with the JMD of tropomyosin receptor kinase A (TrkA). We find that PIP<sub>2 </sub>lipids engage in lasting binding to multiple basic residues and compete with salt bridge within the peptide. We discover three residues insertion into the membrane, and perturb it through computationally designed point mutations. Single-molecule experiments indicate the contribution from hydrophobic insertion is comparable to electrostatic binding, and in-cell experiments show that enhanced TrkA-JMD insertion promotes receptor ubiquitination. Our joint work points to a scenario where basic and hydrophobic residues on disordered domains interact with lipid headgroups and tails, respectively, to restrain flexibility and potentially modulate protein function.</p>

Interaction of sulphone based reactive dyes with cationic surfactant: a spectroscopic and conductometric study

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Misbah Iram ◽  
Hamadia Sultana ◽  
Muhammad Usman ◽  
Bazgha Ahmad ◽  
Nadia Akram ◽  
...  
Keyword(s):  
Strong Interaction ◽  
Cetyltrimethylammonium Bromide ◽  
Hydrophobic Interactions ◽  
Reactive Dyes ◽  
Micellar System ◽  
Palisade Layer ◽  
Micellar Systems ◽  
Gibbs Energies ◽  
Electrostatic And Hydrophobic Interactions ◽  
Conductometric Study

Abstract Interaction of sulphone based reactive dyes, designated as dye-1 and dye-2, with cationic micellar system of cetyltrimethylammonium bromide (CTAB), has been investigated by spectroscopic and conductometeric measurements. Efficiency of the selected micellar systems is assessed by the values of binding constant (K b ), partition coefficient (K x ) and respective Gibbs energies. Critical micelle concentration (CMC) of surfactant, electrostatic and hydrophobic interactions as well as polarity of the medium plays significant role in this phenomenon. The negative values of Gibbs energies of binding (∆G b ) and partition (∆G p ) predicts the feasibility and spontaneity of respective processes. Similarly negative values of ∆G m and ∆H m and positive values of ∆S m , calculated from conductometeric data, further, revealed the exothermicity, spontaneity and, thus, stability of system. The results, herein, have disclosed the strong interaction between dye and surfactant molecules. The dye-2 has been observed to be solubilized to greater extent, as compared to dye 1, due to strong interaction ith hydrophiles of CTAB and accommodation of its molecules in palisade layer of micelle closer to the micelle/water interface.

scholarly journals Interaction of caldesmon with phospholipids

1993 ◽  
Vol 291 (2) ◽  
pp. 403-408 ◽  
Author(s):  
E A Czuryło ◽  
J Zborowski ◽  
R Dabrowska
Keyword(s):  
Fluorescence Spectroscopy ◽  
Hydrophobic Interactions ◽  
Tryptophan Fluorescence ◽  
Terminal Part ◽  
Strong Binding ◽  
Terminal Fragment ◽  
Electrostatic And Hydrophobic Interactions ◽  
The Stability

The interaction of caldesmon with liposomes composed of various phospholipids has been examined by tryptophan fluorescence spectroscopy. The results indicate that caldesmon makes its strongest complex with phosphatidylserine (PS) vesicles (Kass. = 1.45 x 10(5) M-1). Both electrostatic and hydrophobic interactions contribute to the stability of this complex. The site for strong binding of PS seems to be located in the N-terminal part of the 34 kDa C-terminal fragment of caldesmon. Binding of PS at this site results in displacement of calmodulin from its complex with caldesmon.

Contribution of electrostatic and hydrophobic interactions to the adsorption of proteins by aluminium-containing adjuvants

Vaccine ◽  
1995 ◽  
Vol 13 (1) ◽  
pp. 41-44 ◽  
Author(s):  
Ragheb H. Al-Shakhshir ◽  
Fred E. Regnier ◽  
Joe L. White ◽  
Stanley L. Hem
Keyword(s):  
Hydrophobic Interactions ◽  
Electrostatic And Hydrophobic Interactions

The Adsorption Mechanism of Sodium Lignosulfonate on Al2O3 Particle in the Aqueous Solution

2012 ◽  
Vol 550-553 ◽  
pp. 1120-1123
Author(s):  
Rong Li ◽  
Dong Jie Yang ◽  
Wen Yuan Guo ◽  
Xue Qing Qiu
Keyword(s):  
Aqueous Solution ◽  
Hydrogen Bond ◽  
Driving Force ◽  
Adsorption Mechanism ◽  
Hydrophobic Interactions ◽  
Adsorption Properties ◽  
Sodium Lignosulfonate ◽  
Ph Values ◽  
Electrostatic And Hydrophobic Interactions ◽  
Monolayer Coverage

The adsorption properties of sodium lignosulfonate (SL) on Al2O3 particles under different pH values have been investigated. Results show that at low pHs, SL adsorbs on the Al2O3 particles in the form of aggregate as dosage of SL increases; at high pHs, the adsorption is approximately monolayer coverage. With pH values ranging from 3 to 11, the adsorption results are found to be not significantly affected by the addition of urea, ruling out the hydrogen bond as the controlling factor. The paper demonstrates that the main driving force of adsorption is considered as the synergistic effect of electrostatic and hydrophobic interactions when pH pHIEP with additives of Na2SO4 and NaCl.

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