scholarly journals Phase separation and dynamical arrest for particles interacting with mixed potentials—the case of globular proteins revisited

Soft Matter ◽  
2011 ◽  
Vol 7 (3) ◽  
pp. 857-860 ◽  
Author(s):  
Thomas Gibaud ◽  
Frédéric Cardinaux ◽  
Johan Bergenholtz ◽  
Anna Stradner ◽  
Peter Schurtenberger
Keyword(s):  
Phase Separation ◽  
Globular Proteins ◽  
Mixed Potentials

Aggregation, gelation and phase separation of heat denatured globular proteins

2002 ◽  
Vol 304 (1-2) ◽  
pp. 253-265 ◽  
Author(s):  
Dominique Durand ◽  
Jean Christophe Gimel ◽  
Taco Nicolai
Keyword(s):  
Phase Separation ◽  
Globular Proteins

scholarly journals Sequence Grammar Underlying Unfolding and Phase Separation of Globular Proteins

2021 ◽  
Author(s):  
Kiersten M. Ruff ◽  
Yoon Hee Choi ◽  
Dezerae Cox ◽  
Angelique R. Ormsby ◽  
Yoochan Myung ◽  
...  
Keyword(s):  
Phase Separation ◽  
Globular Proteins

scholarly journals Ionic polypeptide tags for protein phase separation

2019 ◽  
Vol 10 (9) ◽  
pp. 2700-2707 ◽  
Author(s):  
Rachel A. Kapelner ◽  
Allie C. Obermeyer
Keyword(s):  
Phase Separation ◽  
Globular Proteins ◽  
Complex Coacervation ◽  
Protein Activity ◽  
Physiological Conditions

Short ionic polypeptide tags were demonstrated to drive complex coacervation of globular proteins at physiological conditions while maintaining protein activity.

scholarly journals Critical adsorption of multiple polyelectrolytes onto a nanosphere: splitting the adsorption–desorption transition boundary

2020 ◽  
Vol 17 (167) ◽  
pp. 20200199 ◽  
Author(s):  
Daniel L. Z. Caetano ◽  
Sidney J. de Carvalho ◽  
Ralf Metzler ◽  
Andrey G. Cherstvy
Keyword(s):  
Phase Separation ◽  
Surface Charge Density ◽  
Globular Proteins ◽  
Spherical Nanoparticles ◽  
Separation Curve ◽  
Low Salt ◽  
Electrostatic Binding ◽  
Adsorption Desorption ◽  
Oppositely Charged ◽  
Added Salt

Employing extensive Monte Carlo computer simulations, we investigate in detail the properties of multichain adsorption of charged flexible polyelectrolytes (PEs) onto oppositely charged spherical nanoparticles (SNPs). We quantify the conditions of critical adsorption—the phase-separation curve between the adsorbed and desorbed states of the PEs—as a function of the SNP surface-charge density and the concentration of added salt. We study the degree of fluctuations of the PE–SNP electrostatic binding energy, which we use to quantify the emergence of the phase subtransitions, including a series of partially adsorbed PE configurations. We demonstrate how the phase-separation adsorption–desorption boundary shifts and splits into multiple subtransitions at low-salt conditions, thereby generalizing and extending the results for critical adsorption of a single PE onto the SNP. The current findings are relevant for finite concentrations of PEs around the attracting SNP, such as the conditions for PE adsorption onto globular proteins carrying opposite electric charges.

N-terminal domain of TDP43 enhances liquid-liquid phase separation of globular proteins

2021 ◽  
pp. 166948
Author(s):  
G. Campbell Carter ◽  
Chia-Heng Hsiung ◽  
Leman Simpson ◽  
Haopeng Yang ◽  
Xin Zhang
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Globular Proteins ◽  
Liquid Phase Separation ◽  
Terminal Domain ◽  
Liquid Liquid Phase Separation

scholarly journals Sequence grammar underlying unfolding and phase separation of globular proteins

2021 ◽  
Author(s):  
Kiersten M Ruff ◽  
Yoon Hee Choi ◽  
Dezerae Cox ◽  
Angelique Royale Ormsby ◽  
Yoochan Myung ◽  
...  
Keyword(s):  
Phase Separation ◽  
Globular Proteins ◽  
Protein Homeostasis ◽  
Superoxide Dismutase 1 ◽  
Unfolded Proteins ◽  
Deposit Formation ◽  
Unfolded Protein ◽  
Protein Deposits ◽  
Model Protein ◽  
Protein Rich

Protein homeostasis involves regulation of the concentrations of unfolded states of globular proteins. Dysregulation can cause phase separation leading to protein-rich deposits. Here, we uncover the sequence-grammar that influences the triad of folding, binding, and phase equilibria of unfolded proteins in cells. We find that the interactions that drive deposit formation of ALS-associated superoxide dismutase 1 mutations are akin to those that drive phase separation and deposit formation in variants of a model protein, barnase. We examined a set of barnase variants to uncover the molecular interactions that drive phase separation of unfolded proteins and formation of unfolded protein deposits (UPODs). The formation of UPODs requires protein destabilization, to increase the concentration of unfolded states, and a requisite sequence grammar to enable cohesive interactions among unfolded proteins. We further find that molecular chaperones, Hsp40 and Hsp70, destabilize UPODs by binding preferentially to and processing unfolded proteins in the dilute phase.

Iso-scattering points during heat-induced aggregation and gelation of globular proteins indicating micro-phase separation

2006 ◽  
Vol 73 (2) ◽  
pp. 299-305 ◽  
Author(s):  
T Nicolai ◽  
M Pouzot ◽  
D Durand ◽  
M Weijers ◽  
R. W Visschers
Keyword(s):  
Phase Separation ◽  
Globular Proteins ◽  
Induced Aggregation

scholarly journals Studying the mechanism of phase separation in aqueous solutions of globular proteins via molecular dynamics computer simulations

2021 ◽  
Vol 23 (1) ◽  
pp. 415-424 ◽  
Author(s):  
Sandi Brudar ◽  
Jure Gujt ◽  
Eckhard Spohr ◽  
Barbara Hribar-Lee
Keyword(s):  
Molecular Dynamics ◽  
Phase Separation ◽  
Aqueous Solutions ◽  
Computer Simulations ◽  
Biological Process ◽  
Globular Proteins ◽  
Living Cells ◽  
P Proteins

Proteins are the most abundant biomacromolecules in living cells, where they perform vital roles in virtually every biological process.

Albumins as Embedding Media for Electron Microscopy

1969 ◽  
Vol 27 ◽  
pp. 422-423 ◽  
Author(s):  
J. L. Farrant ◽  
J. D. McLean
Keyword(s):  
Electron Microscopy ◽  
Electron Microscope ◽  
High Temperature ◽  
Biological Material ◽  
Globular Proteins ◽  
The Past ◽  
Antibody Staining ◽  
Thin Sectioning ◽  
Embedding Medium

For electron microscope techniques such as ferritin-labeled antibody staining it would be advantageous to have available a simple means of thin sectioning biological material without subjecting it to lipid solvents, impregnation with plastic monomers and their subsequent polymerization. With this aim in view we have re-examined the use of protein as an embedding medium. Gelatin which has been used in the past is not very satisfactory both because of its fibrous nature and the high temperature necessary to keep its solutions fluid. We have found that globular proteins such as the serum and egg albumins can be cross-linked so as to yield blocks which are suitable for ultrathin sectioning.

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