scholarly journals Main phase transition in lipid bilayers: Phase coexistence and line tension in a soft, solvent-free, coarse-grained model

2010 ◽  
Vol 132 (15) ◽  
pp. 155104 ◽  
Author(s):  
Martin Hömberg ◽  
Marcus Müller
Keyword(s):  
Phase Transition ◽  
Lipid Bilayers ◽  
Line Tension ◽  
Phase Coexistence ◽  
Solvent Free ◽  
Main Phase ◽  
Coarse Grained ◽  
Coarse Grained Model

scholarly journals High-Resolution, Solvent-Free Coarse-Grained Model for Protein-Lipid Interactions

2011 ◽  
Vol 100 (3) ◽  
pp. 640a
Author(s):  
Tristan Bereau ◽  
Zun-Jing Wang ◽  
Markus Deserno
Keyword(s):  
High Resolution ◽  
Solvent Free ◽  
Coarse Grained ◽  
Lipid Interactions ◽  
Coarse Grained Model

scholarly journals The Globular State of the Single-Stranded RNA: Effect of the Secondary Structure Rearrangements

2015 ◽  
Vol 2015 ◽  
pp. 1-6
Author(s):  
Zareh A. Grigoryan ◽  
Armen T. Karapetian
Keyword(s):  
Phase Transition ◽  
Secondary Structure ◽  
Characteristic Time ◽  
Tertiary Structure ◽  
Mutual Influence ◽  
Coarse Grained ◽  
Nonequilibrium Phase Transition ◽  
Nonequilibrium Phase ◽  
Coarse Grained Model ◽  
Structure Rearrangement

The mutual influence of the slow rearrangements of secondary structure and fast collapse of the long single-stranded RNA (ssRNA) in approximation of coarse-grained model is studied with analytic calculations. It is assumed that the characteristic time of the secondary structure rearrangement is much longer than that for the formation of the tertiary structure. A nonequilibrium phase transition of the 2nd order has been observed.

Supported Lipid Bilayers on Mica and Silicon Oxide: Comparison of the Main Phase Transition Behavior

2010 ◽  
Vol 114 (27) ◽  
pp. 8926-8933 ◽  
Author(s):  
Heiko M. Seeger ◽  
Alessandro Di Cerbo ◽  
Andrea Alessandrini ◽  
Paolo Facci
Keyword(s):  
Phase Transition ◽  
Lipid Bilayers ◽  
Silicon Oxide ◽  
Main Phase ◽  
Supported Lipid Bilayers ◽  
Phase Transition Behavior ◽  
Transition Behavior

scholarly journals Understanding the Phase Behavior of Coarse-Grained Model Lipid Bilayers through Computational Calorimetry

2012 ◽  
Vol 116 (5) ◽  
pp. 1551-1569 ◽  
Author(s):  
Jocelyn M. Rodgers ◽  
Jesper Sørensen ◽  
Frédérick J.-M. de Meyer ◽  
Birgit Schiøtt ◽  
Berend Smit
Keyword(s):  
Phase Behavior ◽  
Lipid Bilayers ◽  
Coarse Grained ◽  
Coarse Grained Model

One-particle-thick, solvent-free, coarse-grained model for biological and biomimetic fluid membranes

2010 ◽  
Vol 82 (1) ◽  
Author(s):  
Hongyan Yuan ◽  
Changjin Huang ◽  
Ju Li ◽  
George Lykotrafitis ◽  
Sulin Zhang
Keyword(s):  
Solvent Free ◽  
Coarse Grained ◽  
Coarse Grained Model ◽  
Fluid Membranes

scholarly journals Kinetic frustration by limited bond availability controls the LAT protein condensation phase transition on membranes

2021 ◽  
Author(s):  
Simou Sun ◽  
Trevor GrandPre ◽  
David T. Limmer ◽  
Jay T. Groves
Keyword(s):  
Phase Transition ◽  
T Cell Activation ◽  
Protein Interactions ◽  
Cell Activation ◽  
Coarse Grained ◽  
Structural Basis ◽  
Protein Protein Interactions ◽  
Kinetic Measurements ◽  
Coarse Grained Model ◽  
Intrinsically Disordered

AbstractLAT is a membrane-linked scaffold protein that undergoes a phase transition to form a two-dimensional protein condensate on the membrane during T cell activation. Governed by tyrosine phosphorylation, LAT recruits various proteins that ultimately enable condensation through a percolation network of discrete and selective protein-protein interactions. Here we describe detailed kinetic measurements of the phase transition, along with coarse-grained model simulations, that reveal LAT condensation is kinetically frustrated by the availability of bonds to form the network. Unlike typical miscibility transitions in which compact domains may coexist at equilibrium, the LAT condensates are dynamically arrested in extended states, kinetically trapped out of equilibrium. Modeling identifies the structural basis for this kinetic arrest as the formation of spindle arrangements, favored by limited multivalent binding interactions along the flexible, intrinsically disordered LAT protein. These results reveal how local factors controlling the kinetics of LAT condensation enable formation of different, stable condensates, which may ultimately coexist within the cell.

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