Related Experiment Video
Updated: Jan 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
Chemometric evaluation of key residues affecting the stability of cold shock proteins
Jack E Buckley1, Nathaniel J Zbacnik1, Charles S Henry2
1Legacy BioDesign LLC, Johnstown, CO 80534, USA.
Abstract:
Reduced properties, also known as amino acid descriptors, quantify changes in physicochemical properties of amino acids upon mutation. Combined with PLS (partial least squares) modeling, the impact of various mutations on the conformational stability of cold shock proteins (CSPs) was examined. Consistent with the initial evaluation of these systems, electrostatic properties at a select number of central residues were found to govern the conformational stability of CSP mutants. In addition, the current studies found that packing efficiency within the β-sheet core and flexibility of the peptide backbone also contribute to the overall stability of these small proteins.
More Related Videos
08:13Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
19:16The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
Published on: March 17, 2010
Related Concept Videos
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...
Bacterial Protein Maturation
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Protein Denaturation
Molecular Chaperones and Protein Folding
The...