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ProTherm: 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 10, 1998
PubMed
Summary

The ProTherm database offers over 3300 thermodynamic and structural data points for proteins and mutants, aiding protein stability research. It features a user-friendly interface and links to other biological databases.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Protein stability is crucial for biological function.
  • Understanding protein thermodynamics aids in deciphering mutation effects.

Purpose of the Study:

  • To introduce the first release of the Thermodynamic Database for Proteins and Mutants (ProTherm).
  • To provide a comprehensive resource for protein thermodynamic and structural data.

Main Methods:

  • Compilation of over 3300 data entries for wild type and mutant proteins.
  • Inclusion of thermodynamic parameters (e.g., Gibbs free energy change, enthalpy, heat capacity) and structural information.
  • Development of a WWW interface for data searching and retrieval.

Main Results:

Related Experiment Videos

  • ProTherm contains extensive data on protein stability parameters.
  • The database integrates structural details, experimental conditions, and links to external databases (PubMed, PDB).
  • Automated mapping of mutation sites to PDB structures is available.

Conclusions:

  • ProTherm serves as a valuable resource for researchers studying protein stability and mutations.
  • The database facilitates integrated analysis of thermodynamic, structural, and mutation data.
  • Enhanced data accessibility and cross-linking improve research efficiency.