Related Experiment Video
Updated: Oct 29, 2025
08:46
Implementation of In Vitro Drug Resistance Assays: Maximizing the Potential for Uncovering Clinically Relevant Resistance Mechanisms
Published on: December 9, 2015
10.8K
Performance of Web tools for predicting changes in protein stability caused by mutations.
Anna Marabotti1, Eugenio Del Prete2, Bernardina Scafuri3
1Department of Chemistry and Biology "A. Zambelli", University of Salerno, Fisciano, SA, Italy. amarabotti@unisa.it.
BMC Bioinformatics
|July 6, 2021
Summary
Predicting protein stability changes from mutations remains challenging. Combining multiple prediction tools offers a more reliable approach, though current methods still have limitations.
Area of Science:
- Biochemistry
- Computational Biology
- Protein Science
Background:
- Developing web tools to predict protein thermodynamic stability changes due to mutations has been ongoing for decades.
- Accurate prediction of these stability changes remains a significant challenge in the field.
Purpose of the Study:
- To assess the reliability of five recently developed web tools for predicting mutation-induced changes in protein thermodynamic stability.
- To evaluate the progress made in the field of computational prediction of protein stability.
Main Methods:
- Evaluation of five distinct web-based prediction tools.
- Analysis of prediction accuracy, focusing on biases and reliability intervals.
Main Results:
- Despite improvements, current predictors are not ideal, showing bias towards destabilizing mutations.
- Predictions are generally unreliable for mutations causing a change in Gibbs free energy (ΔΔG) within ±0.5 kcal/mol.
- A consensus approach, combining results from multiple predictors, offers a practical method to enhance prediction reliability.
Conclusions:
- Future tool development should prioritize balanced datasets for training predictors.
- Users are advised to integrate results from multiple prediction tools for improved accuracy in assessing mutation effects on protein thermodynamic stability.
More Related Videos
Related Concept Videos
02:26Conservation of Protein Domains Over Different Proteins
13.4K
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
13.4K
01:49Conserved Binding Sites
4.7K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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...
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...
4.7K
01:28Protein Denaturation
7.5K
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
7.5K