Related Experiment Video
Updated: May 14, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Determining the conformational stability of a protein from urea and thermal unfolding curves
Gerald R Grimsley1, Saul R Trevino, Richard L Thurlkill
1Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, Texas, USA.
Abstract:
This unit contains basic protocols for determining the conformational stability of a globular protein from either urea or thermal unfolding curves. Circular dichroism is the optical spectroscopic technique most commonly used to monitor protein unfolding. The protocols describe how to analyze data from an unfolding curve to obtain the thermodynamic parameters necessary to calculate conformational stability, and how to determine differences in stability between protein variants.
More Related Videos
07:22How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
Published on: February 11, 2019
08:13Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
Related Concept Videos
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Folding
Protein Denaturation
Molecular Chaperones and Protein Folding
The...
Protein Folding Quality Check in the RER