Related Experiment Video
Updated: May 25, 2026
07:22
How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
Published on: February 11, 2019
Generic pathways to stability in concentrated protein mixtures.
Ilja K Voets1, Veronique Trappe, Peter Schurtenberger
1Institute for Complex Molecular Systems and Laboratory of Macromolecular and Organic Chemistry, Eindhoven University of Technology, P.O. Box 513, 5600 MB Eindhoven, The Netherlands. i.voets@tue.nl
Physical Chemistry Chemical Physics : PCCP
|January 21, 2012
Summary
Ionic strength and protein composition control protein mixture phase behavior. Intermediate salt concentrations suppress phase separation and crystallization by influencing counter-ion entropy, crucial for cytosol stability.
Area of Science:
- Biophysics
- Physical Chemistry
- Biochemistry
Background:
- Protein mixtures exhibit complex phase behavior.
- Understanding these behaviors is vital for biological systems like the cytosol.
Purpose of the Study:
- To investigate the influence of ionic strength and partial volume fractions on protein mixture phase behavior.
- To elucidate the thermodynamic principles governing protein phase separation and crystallization.
Main Methods:
- Experimental analysis of binary protein mixtures.
- Thermodynamic modeling of protein-counter-ion interactions.
Main Results:
- Ionic strength dictates the contribution of counter-ion entropy to system thermodynamics.
- Phase separation at low ionic strength and crystallization at high ionic strength are suppressed at intermediate salt concentrations.
- Partial volume fraction of crystallizing protein influences crystallization boundaries; co-existing proteins delay crystallization.
Conclusions:
- Protein mixture stability is governed by ionic strength and composition, not solely protein-specific properties.
- Findings offer insights into the stability of complex biological mixtures like the cytosol.
- Control over protein phase behavior can be achieved through manipulation of salt concentration and protein composition.
More Related Videos
Related Concept Videos
01:27Globular Proteins
In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
01:22Protein Folding
Overview
01:29The Colloidal State
The formation of a colloidal system is exemplified by an aqueous solution containing Cl− ions is introduced to another containing Ag+ ions, resulting in the precipitation of solid AgCl as extremely tiny crystals. Instead of settling out as a filterable precipitate, these crystals remain suspended in the liquid, showcasing a colloidal system.A colloidal system involves colloidal particles within the approximate range of 1 to 1000 nm in at least one dimension, dispersed in a medium called the...
01:09Complexation Equilibria: Factors Influencing Stability of Complexes
In complexation reactions, metal cations are the electron pair acceptors, and the ligands are the electron pair donors. The stability of the metal complexes depends primarily on the complexing ability of the central metal ion and the nature of the ligands. Generally, the complexing ability of the metal ion depends on the size and charge of the ion. As the metal ion size increases, the stability of the metal complexes decreases, provided that the valency of the metal ion and the ligands remain...
01:26Bacterial Protein Maturation
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
01:29Amino Acid Biosynthetic Pathways
Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which provide...