Related Experiment Video
Updated: Jun 19, 2026

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
THE EFFECT OF DENATURATION ON THE VISCOSITY OF PROTEIN SYSTEMS
1Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J., and the Hospital of The Rockefeller Institute for Medical Research, New York.
Abstract:
The viscosity of a protein solution is increased by the denaturation of the protein. This is true both when there is the formation of protein aggregates which occlude water and when there is no aggregation. Under certain conditions, as a result of the aggregation following denaturation, a solution containing only one per cent of protein may be converted into a clear gel. The conditions for obtaining very viscous solutions containing little denatured protein are always close to the conditions for actual precipitation and under these conditions the viscosity is very sensitive to slight changes in the concentration of salts and hydrogen ions.
Related Concept Videos
Protein Denaturation
Viscosity of Fluid
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Surface Tension, Capillary Action, and Viscosity
The various IMFs between identical molecules of a substance are examples of cohesive forces. The molecules within a liquid are surrounded by other molecules and are attracted equally in all directions by the cohesive forces within the liquid. However, the molecules on the surface of a liquid are attracted only by about one-half as many molecules. Because of the unbalanced molecular attractions on the surface molecules, liquids contract to form a shape that minimizes the number...
SDS-PAGE
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...

