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

ProTherm, Thermodynamic Database for Proteins and Mutants: developments in version 3.0.

M Michael Gromiha1, Hatsuho Uedaira, Jianghong An

  • 1RIKEN Tsukuba Institute, Institute of Physical and Chemical Research, 3-1-1 Koyadai, Tsukuba, Ibaraki 305-0074, Japan.

Nucleic Acids Research
|December 26, 2001
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

PDA-MutPred: Reliable prediction of binding affinity change upon mutation in protein-DNA complexes.

International journal of biological macromolecules·2026
Same author

Classification of driver and passenger mutations in different cancer types using deep neural networks.

Bioinformatics advances·2026
Same author

Investigating protein aggregation in protein-carbohydrate interfaces using sequence and structural features.

Biochimica et biophysica acta. Proteins and proteomics·2026
Same author

Integrating Sequence, Structure, and Graph-based Features for Elucidating the Stability of Thermophilic Proteins.

Journal of molecular biology·2025
Same author

Identification of Compound Heterozygous CYP11A1 Variants via Reanalysis of Clinical Sequencing Data.

American journal of medical genetics. Part A·2025
Same author

Herpes Simplex Virus Glycoprotein D Associated with Aβ<sub>1-42</sub> Tetramers Mediates Neurotoxicity by Perturbing Neuronal Membrane Integrity: A Molecular Dynamics Simulation.

ACS chemical neuroscience·2025

The ProTherm database now offers over 10,000 thermodynamic data points for proteins and mutants, significantly expanding its scope. This enhanced version improves data accessibility and integration with other biological databases.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Protein thermodynamic data is crucial for understanding protein stability and function.
  • Existing databases may lack comprehensive information on protein mutants and their thermodynamic properties.

Purpose of the Study:

  • To present the updated release of the ProTherm database, a thermodynamic database for proteins and mutants.
  • To highlight the expanded data content and new search functionalities.
  • To emphasize the integration of ProTherm with other biological databases.

Main Methods:

  • Compilation of thermodynamic parameters, experimental conditions, and protein information.
  • Inclusion of structural, functional, and literature data for proteins and mutants.

Related Experiment Videos

  • Development of enhanced search options based on PDB code, number of states, and reversibility.

    • Main Results:

    • The database now contains over 10,000 numerical data points, a 300% increase from the first version.
    • Added protein source information, SWISS-PROT, Protein Information Resource, and Protein Data Bank (PDB) codes.
    • Implemented cross-linking with sequence, structural, functional, and literature databases, with automatic mapping of mutant sites.

    Conclusions:

    • The updated ProTherm database provides a significantly expanded and integrated resource for protein thermodynamic data.
    • Enhanced search capabilities and database linkages improve data retrieval and analysis for researchers.
    • ProTherm serves as a valuable, freely accessible tool for studying protein folding and stability.