Decrease of dielectric constant transforms the protein molecule into the molten globule state
Related Experiment Video
Updated: Oct 13, 2026

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
Published on: November 21, 2010
1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia.
Abstract:
The effect of organic solvents of different nature (alcohols, amides, and cyclic ethers) on the structural properties of beta-lactoglobulin was studied by circular dichroism and fluorescence spectroscopy. It is shown that the protein molecule undergoes at least two consecutive conformational transitions upon increase of the organic solvent concentration. Denaturation of the protein molecule occurs in the first step and a transition into the highly helical non-compact state in the second. In other words, under such conditions a compact denatured intermediate state is formed with a pronounced secondary structure, i.e., a molten globule-like state. It is shown that decrease of the dielectric constant of the media is responsible for structural changes of the protein molecule.
Related Concept Videos
Protein Folding
Membrane Fluidity
Protein Diffusion in the Membrane
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Globular 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...
Protein Denaturation

