Liquid–liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protein condensation diseases to subcellular organization to possible pathways toward protein crystallization. Understanding and controlling LLPS in proteins is therefore highly relevant for various areas of (biological) soft matter research. Solutions of the protein bovine serum albumin (BSA) have been shown to have a lower critical solution temperature–LLPS (LCST–LLPS) induceable by multivalent salts. Importantly, the nature of the multivalent cation used influences the LCST–LLPS in such systems. Here, we present a systematic ultrasmall-angle X-ray scattering investigation of the kinetics of LCST–LLPS of BSA in the presence of different mixtures ...
Phase transitions of protein aqueous solutions are important for protein crystallization and biomate...
We present a series of experimental results that disclose the crucial role of ionic strength and par...
Thermal-induced conformational changes and protein-protein interactions of bovine serum albumin (BSA...
Liquid-liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
Liquid–liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
In the presence of trivalent cations, negatively charged globular proteins show a rich phase behavio...
We study the kinetics of the liquid–liquid phase separation (LLPS) and its arrest in protein solutio...
Protein phase behaviour is of importance in various areas of research such as structural biology, ra...
We present an experimental study combined with a theoretical discussion of the effective interaction...
Intermolecular interactions in protein solutions, in general, contain many contributions. If short-r...
The interplay of the glass transition with liquid-liquid phase separation (LLPS) is a subject of int...
The protein human serum albumin (HSA) is able to readily crystallize in the presence of trivalent ca...
In all areas related to protein adsorption, from medicine to biotechnology to heterogeneous nucleati...
Understanding the fundamental process of liquid--liquid phase separation (LLPS) in biological system...
Phase transitions of protein aqueous solutions are important for protein crystallization and biomate...
We present a series of experimental results that disclose the crucial role of ionic strength and par...
Thermal-induced conformational changes and protein-protein interactions of bovine serum albumin (BSA...
Liquid-liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
Liquid–liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
In the presence of trivalent cations, negatively charged globular proteins show a rich phase behavio...
We study the kinetics of the liquid–liquid phase separation (LLPS) and its arrest in protein solutio...
Protein phase behaviour is of importance in various areas of research such as structural biology, ra...
We present an experimental study combined with a theoretical discussion of the effective interaction...
Intermolecular interactions in protein solutions, in general, contain many contributions. If short-r...
The interplay of the glass transition with liquid-liquid phase separation (LLPS) is a subject of int...
The protein human serum albumin (HSA) is able to readily crystallize in the presence of trivalent ca...
In all areas related to protein adsorption, from medicine to biotechnology to heterogeneous nucleati...
Understanding the fundamental process of liquid--liquid phase separation (LLPS) in biological system...
Phase transitions of protein aqueous solutions are important for protein crystallization and biomate...
We present a series of experimental results that disclose the crucial role of ionic strength and par...
Thermal-induced conformational changes and protein-protein interactions of bovine serum albumin (BSA...