ProThermDB

ProThermDB provides thermodynamic data for proteins and protein mutants to support analysis of protein stability and folding.

Key Features:

• Extensive Data Collection: Contains approximately 31,500 entries and over 120,000 thermodynamic parameters, representing an 84% expansion relative to the original ProTherm.
• Data Sources: Includes data derived using high-throughput proteomics techniques employing whole-cell approaches and literature-reported experiments.
• Diverse Thermodynamic Parameters: Reports melting temperature, free energy (measured through thermal and denaturant denaturation), enthalpy change, and heat capacity change for proteins and mutants.
• Experimental Context: Associates each entry with detailed experimental methods and conditions to enable comparative analyses and replication.
• Sequence and Structural Information: Integrates sequence and structural data to relate mutations to stability at molecular and structural levels.
• Literature Integration: Cross-links entries to PDB, UniProt, and PubMed for access to structural records and source publications.

Scientific Applications:

• Protein Engineering: Supports design and evaluation of mutations to modify protein stability using reported thermodynamic parameters.
• Mutational Analysis: Enables analysis of the effects of specific amino acid substitutions on protein folding and stability.
• Comparative Studies: Facilitates comparison of thermodynamic parameters across proteins, mutants, organisms, and cell lines for evolutionary and functional investigations.

Methodology:

Collects thermodynamic parameters measured by thermal and denaturant denaturation (melting temperature, ΔG, ΔH, ΔCp), integrates sequence and structural data, and cross-links entries to PDB, UniProt, and PubMed; includes data derived from high-throughput proteomics employing whole-cell approaches.