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Related Experiment Videos

ProTherm, version 2.0: thermodynamic database for proteins and mutants.

M M Gromiha1, J An, H Kono

  • 1Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), 3-1-1 Koyadai, Tsukuba, Ibaraki 305-0074, Japan.

Nucleic Acids Research
|December 11, 1999
PubMed
Summary

The ProTherm 2.0 database now offers over 5500 entries on protein thermodynamic parameters and mutant data. This enhanced release provides richer details and improved search functionalities for researchers studying protein thermodynamics.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Protein thermodynamic data is crucial for understanding protein stability and function.
  • Databases compiling this information are essential resources for researchers.
  • Previous versions of ProTherm provided valuable, but limited, thermodynamic and structural data.

Purpose of the Study:

  • To release the second version of the Thermo-dynamic Database for Proteins and Mutants (ProTherm 2.0).
  • To expand the database with increased entries and enhanced data points.
  • To improve data accessibility and integration with other biological databases.

Main Methods:

  • Compilation of numerical thermodynamic parameters, structural information, experimental conditions, and literature data.

Related Experiment Videos

  • Inclusion of data on reversibility, buffer/ion concentrations, and spatial arrangement of surrounding residues for mutants.
  • Development of a World Wide Web (WWW) interface for data searching and sorting.
  • Integration with structural and literature databases, with visualization tools.

    • Main Results:

    • ProTherm 2.0 contains over 5500 entries, a 67% increase from the previous version.
    • New data includes reversibility, buffer/ion concentrations, and surrounding residue information.
    • Enhanced WWW interface allows diverse search conditions and sorting options.
    • Direct links to structural databases and 3D visualization of mutation sites are available.

    Conclusions:

    • ProTherm 2.0 represents a significant expansion of protein thermodynamic and mutant data.
    • The enhanced features improve usability and data integration for researchers.
    • The database serves as a comprehensive, freely accessible resource for the scientific community.