A response to the comments concerning “(liquid+liquid) phase behaviour for systems containing (aromatic+TBA+methylcyclohexane)”

2005 ◽  
Vol 37 (4) ◽  
pp. 393
Author(s):  
H. Ghanadzadeh ◽  
A. Ghanadzadeh
Keyword(s):  
Liquid Phase ◽  
Phase Behaviour

scholarly journals Expansion of Intrinsically Disordered Proteins Increases the Range of Stability of Liquid–Liquid Phase Separation

Molecules ◽  
2020 ◽  
Vol 25 (20) ◽  
pp. 4705
Author(s):  
Adiran Garaizar ◽  
Ignacio Sanchez-Burgos ◽  
Rosana Collepardo-Guevara ◽  
Jorge R. Espinosa
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Protein Interactions ◽  
Conformational Dynamics ◽  
Liquid Phase Separation ◽  
Phase Behaviour ◽  
Coarse Grained ◽  
Protein Protein Interactions ◽  
Intrinsically Disordered ◽  
Liquid Liquid Phase Separation

Proteins containing intrinsically disordered regions (IDRs) are ubiquitous within biomolecular condensates, which are liquid-like compartments within cells formed through liquid–liquid phase separation (LLPS). The sequence of amino acids of a protein encodes its phase behaviour, not only by establishing the patterning and chemical nature (e.g., hydrophobic, polar, charged) of the various binding sites that facilitate multivalent interactions, but also by dictating the protein conformational dynamics. Besides behaving as random coils, IDRs can exhibit a wide-range of structural behaviours, including conformational switching, where they transition between alternate conformational ensembles. Using Molecular Dynamics simulations of a minimal coarse-grained model for IDRs, we show that the role of protein conformation has a non-trivial effect in the liquid–liquid phase behaviour of IDRs. When an IDR transitions to a conformational ensemble enriched in disordered extended states, LLPS is enhanced. In contrast, IDRs that switch to ensembles that preferentially sample more compact and structured states show inhibited LLPS. This occurs because extended and disordered protein conformations facilitate LLPS-stabilising multivalent protein–protein interactions by reducing steric hindrance; thereby, such conformations maximize the molecular connectivity of the condensed liquid network. Extended protein configurations promote phase separation regardless of whether LLPS is driven by homotypic and/or heterotypic protein–protein interactions. This study sheds light on the link between the dynamic conformational plasticity of IDRs and their liquid–liquid phase behaviour.

Liquid-phase behaviour of normal spectral emissivity at 684.5 nm of some selected metals

2002 ◽  
Vol 34 (6) ◽  
pp. 669-679 ◽  
Author(s):  
Claus Cagran ◽  
Christian Brunner ◽  
Achim Seifter ◽  
Gernot Pottlacher
Keyword(s):  
Liquid Phase ◽  
Spectral Emissivity ◽  
Phase Behaviour ◽  
Normal Spectral Emissivity

Liquid phase behaviour in nonstoichiometric calcium-doped lanthanum chromites

1996 ◽  
Vol 31 (1) ◽  
pp. 157-163 ◽  
Author(s):  
J. D. Carter ◽  
M. M. Nasrallah ◽  
H. U. Anderson
Keyword(s):  
Liquid Phase ◽  
Phase Behaviour ◽  
Calcium Doped ◽  
Lanthanum Chromites

Liquid phase behaviour and thermodynamics of acetone+methanol+n-alkane (C9–C12) mixtures

2003 ◽  
Vol 206 (1-2) ◽  
pp. 61-85 ◽  
Author(s):  
A. Touriño ◽  
L.M. Casás ◽  
G. Marino ◽  
M. Iglesias ◽  
B. Orge ◽  
...  
Keyword(s):  
Liquid Phase ◽  
Phase Behaviour

Liquid–liquid phase behaviour, liquid–liquid density, and interfacial tension of multicomponent systems at 298K

2007 ◽  
Vol 255 (2) ◽  
pp. 147-159 ◽  
Author(s):  
Blanca Estela García-Flores ◽  
Arturo Trejo ◽  
Jacinto Águila-Hernández
Keyword(s):  
Liquid Phase ◽  
Interfacial Tension ◽  
Phase Behaviour ◽  
Liquid Density ◽  
Multicomponent Systems

scholarly journals Effects of solid poly (ethylene glycols) addition to the solutions of aniline or N,N-dimethylaniline with water: Experimental measurements and modeling

2016 ◽  
Vol 81 (7) ◽  
pp. 789-798
Author(s):  
Danijela Soldatovic ◽  
Nikola Grozdanic ◽  
Zoran Visak ◽  
Ivona Radovic ◽  
Mirjana Kijevcanin
Keyword(s):  
Polyethylene Glycol ◽  
Liquid Phase ◽  
Binary Systems ◽  
Ambient Pressure ◽  
Aqueous System ◽  
Phase Behaviour ◽  
Experimental Measurements ◽  
Ethylene Glycols ◽  
Poly Ethylene ◽  
Solid Liquid

In this work, the liquid - liquid and solid - liquid phase behaviour of ten aqueous pseudo-binary and three binary systems containing polyethylene glycol 2050, polyethylene glycol 35000, aniline, N,N-dimethylaniline and water, in the temperature range T = (298.15 to 350.15) K and at ambient pressure of 0.1 MPa, was studied. The obtained temperature-composition phase diagrams showed that the only functional co-solvent was PEG2050 for aniline in water, while PEG35000 even showed a clear anti-solvent effect in the N,N-dimethylaniline aqueous system. The experimental SLE data have been correlated by the Non-Random Two-Liquid (NRTL) model, and the correlation results are in accordance with the experimental results.

scholarly journals Accurate model of liquid-liquid phase behaviour of intrinsically-disordered proteins from data-driven optimization of single-chain properties

2021 ◽  
Author(s):  
Giulio Tesei ◽  
Thea K. Schulze ◽  
Ramon Crehuet ◽  
Kresten Lindorff-Larsen
Keyword(s):  
Liquid Phase ◽  
Intrinsically Disordered Proteins ◽  
Molecular Simulations ◽  
Phase Behaviour ◽  
Data Driven ◽  
Coarse Grained ◽  
Disordered Proteins ◽  
Model Parameters ◽  
Single Chain ◽  
Intrinsically Disordered

Many intrinsically disordered proteins (IDPs) may undergo liquid-liquid phase separation (LLPS) and participate in the formation of membraneless organelles in the cell, thereby contributing to the regulation and compartmentalisation of intracellular biochemical reactions. The phase behaviour of IDPs is sequence-dependent, and its investigation through molecular simulations requires protein models that combine computational efficiency with an accurate description of intra- and intermolecular interactions. We developed a general coarse-grained model of IDPs, with residue-level detail, based on an extensive set of experimental data on single-chain properties. Ensemble-averaged experimental observables are predicted from molecular simulations, and a data-driven parameter-learning procedure is used to identify the residue-specific model parameters that minimize the discrepancy between predictions and experiments. The model accurately reproduces the experimentally observed conformational propensities of a set of IDPs. Through two-body as well as large-scale molecular simulations, we show that the optimization of the intramolecular interactions results in improved predictions of protein self-association and LLPS.

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