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PINT: Protein-protein Interactions Thermodynamic Database.

M D Shaji Kumar1, M Michael Gromiha

  • 1Department of Biochemical Engineering and Science, Kyushu Institute of Technology Iizuka 820-8502, Fukuoka, Japan. shaji@bse.kyutech.ac.jp

Nucleic Acids Research
|December 31, 2005
PubMed
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The Protein-protein Interactions Thermodynamic Database (PINT) offers over 1500 data points on protein binding thermodynamics. This resource aids in understanding protein interaction mechanisms through comprehensive thermodynamic and structural information.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Protein-protein interactions are fundamental to cellular processes.
  • Understanding the thermodynamics of these interactions is crucial for elucidating molecular mechanisms.
  • Existing resources may lack comprehensive thermodynamic data for protein binding.

Purpose of the Study:

  • To introduce the Protein-protein Interactions Thermodynamic Database (PINT) as a novel resource.
  • To provide a centralized repository for thermodynamic parameters of protein-protein interactions.
  • To facilitate research into the mechanisms governing protein binding.

Main Methods:

  • Compilation of >1500 data entries from scientific literature.
  • Inclusion of thermodynamic parameters (e.g., free energy, enthalpy, heat capacity changes).

Related Experiment Videos

  • Integration of sequence, structural, experimental, and literature data.

    • Main Results:

    • PINT v1.0 contains over 1500 entries detailing protein-protein interaction thermodynamics.
    • Each entry includes diverse data: thermodynamic parameters, protein identifiers (PIR, SWISS-PROT, PDB), experimental conditions, and literature links.
    • A web interface allows flexible data searching, selection, and sorting.

    Conclusions:

    • PINT serves as a valuable, freely accessible resource for researchers studying protein-protein interactions.
    • The database facilitates the analysis of binding mechanisms by providing integrated thermodynamic and structural information.
    • Cross-linking with other major databases (PIR, SWISS-PROT, PDB, PubMed) enhances its utility.