MPTherm: database for membrane protein thermodynamics for understanding folding and stability

Area of Science:

• Biochemistry
• Structural Biology
• Bioinformatics

Background:

• Membrane proteins (MPs) are crucial for cellular functions, with their stability intrinsically linked to structure.
• Understanding MP thermodynamics is vital for elucidating structure-function relationships, yet dedicated resources are lacking.
• Factors affecting MP stability are unique due to their membrane-spanning regions, differentiating them from globular proteins.

Purpose of the Study:

• To develop MPTherm, a specialized database for membrane protein thermodynamic data.
• To consolidate and present diverse thermodynamic parameters for a large set of MPs.
• To provide a centralized resource for researchers studying MP stability, function, and drug development.

Main Methods:

• Compilation of over 7000 thermodynamic data points from approximately 320 MPs.
• Inclusion of protein sequence, structural information, membrane topology, and experimental conditions.
• Development of a web-accessible database (MPTherm) with search, display, and visualization functionalities.

Main Results:

• MPTherm database successfully integrates extensive thermodynamic data for 320 MPs.
• The database provides detailed information including melting temperature, free energy, and enthalpy.
• Features include sequence/structure visualization and links to UniProt and PDB.

Conclusions:

• MPTherm serves as a valuable resource for understanding membrane protein stability and function.
• The database can facilitate the development of predictive models for MPs.
• MPTherm aids in identifying potential drug targets for MP-associated diseases.