Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Predicting protein stability changes from sequences using support vector machines.

Emidio Capriotti1, Piero Fariselli, Remo Calabrese

  • 1Laboratory of Biocomputing, CIRB/Department of Biology, University of Bologna Bologna, Italy.

Bioinformatics (Oxford, England)
|October 6, 2005
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Survival prediction from neural parametrization of diffusive processes.

Physical review. E·2026
Same author

Update of the MSKCC nomogram for metastatic progression and its role in active surveillance: the Italian TPCP cohort.

Frontiers in oncology·2026
Same author

Environmental Personal Exposure Clusters to Investigate Multiple Sclerosis and Amyotrophic Lateral Sclerosis Progression.

Studies in health technology and informatics·2026
Same author

On the state of protein function prediction: a report on the fourth CAFA challenge.

bioRxiv : the preprint server for biology·2026
Same author

Molecular-Based Ecosystem to Improve Personalized Medicine in Chronic Myelomonocytic Leukemia.

Journal of clinical oncology : official journal of the American Society of Clinical Oncology·2026
Same author

Open and sustainable AI: challenges, opportunities and the road ahead in the life sciences.

Nature methods·2026
Same journal

3DICE: Interpretable 3D Cross-Modal Learning for Drug-Target Interaction Prediction and Large-Scale Drug Discovery.

Bioinformatics (Oxford, England)·2026
Same journal

KASSPer: Kinase Active Site Structure Prediction using Protein and Ligand Language Models and Its Application to Virtual Screening.

Bioinformatics (Oxford, England)·2026
Same journal

IDR searcher: a search engine solution for public image resources.

Bioinformatics (Oxford, England)·2026
Same journal

KCFtools: Rapid alignment-free method for introgression screening and GWAS using k-mer profiles.

Bioinformatics (Oxford, England)·2026
Same journal

Meta2DB: Curated shotgun metagenomic feature sets and metadata for health state prediction.

Bioinformatics (Oxford, England)·2026
Same journal

conMItion: an R package adjusting confounding factors for associations in multi-omics.

Bioinformatics (Oxford, England)·2026
See all related articles

Predicting protein stability changes from amino acid sequences is now possible. Our new method accurately forecasts mutation impacts on protein stability, aiding disease-related genetic variation studies.

Area of Science:

  • Biochemistry and Molecular Biology
  • Computational Biology
  • Genetics

Background:

  • Protein stability is crucial for understanding protein folding and disease mechanisms.
  • Current prediction methods require atomic structures, limiting large-scale genomic analysis.
  • Sequence-based prediction is essential for genome annotation and studying single nucleotide polymorphisms (SNPs).

Purpose of the Study:

  • To develop a computational method for predicting protein stability changes from amino acid sequences.
  • To assess the accuracy of the prediction method for both the sign and magnitude of stability changes.
  • To evaluate the method's utility in analyzing disease-related mutations.

Main Methods:

  • Support Vector Machines (SVM) algorithm utilized.

Related Experiment Videos

  • Input data: protein sequences.
  • Output: predicted sign and value of free energy stability change (ΔΔG).
  • Main Results:

    • Achieved 77% accuracy in predicting the sign of ΔΔG (protein stability change).
    • Demonstrated satisfactory correlation with experimental data for predicting ΔΔG values.
    • Validated the method on disease-related SNPs, confirming mutations decrease protein stability.

    Conclusions:

    • The developed sequence-based method effectively predicts protein stability changes.
    • This tool aids in understanding the impact of mutations, particularly disease-related SNPs.
    • The findings support the link between decreased protein stability and disease-causing mutations.