Related Experiment Video
Updated: Aug 17, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Acid-induced denaturation and refolding of prothrombin
Dilip Kumar Debnath1, Kasturi Mukhopadhyay, Soumen Basak
1Chemical Sciences Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Calcutta 700064, India.
Abstract:
Structural transitions of the blood coagulation factor prothrombin (extracted from goat blood) in response to reduction of pH were investigated by fluorescence, circular dichroism and light scattering measurements. The study revealed the presence of a partially unfolded state at around pH 3.5, characterized by marked enhancement of fluorescence from ANS bound to the protein, increase of bimolecular rate constant for tryptophan fluorescence quenching and a sharp peak in the light scattering intensity. Further lowering of the pH caused reversal of the trend of variation of these parameters, suggesting that prothrombin folds back to a compact state containing native-like secondary structural elements. The refolded state at low pH (
More Related Videos
10:24Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
11:17Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
Published on: March 10, 2021
Related Concept Videos
Protein Denaturation
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
Molecular Chaperones and Protein Folding
The...
EDTA: Auxiliary Complexing Reagents