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Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
Published on: November 21, 2017
Thermodynamics of stacking interactions in proteins
Simone Marsili1, Riccardo Chelli, Vincenzo Schettino
1Dipartimento di Chimica, Università di Firenze, Sesto Fiorentino, Italy.
Physical Chemistry Chemical Physics : PCCP
|May 10, 2008
Summary
This study investigates pi-pi interactions between protein residues using the Protein Data Bank. Stacked complexes are thermodynamically relevant and common in proteins, influencing their stability.
Area of Science:
- Biochemistry
- Structural Biology
- Computational Biology
Background:
- Proteins are crucial biomolecules with complex structures.
- Interactions between amino acid residues stabilize protein structures.
- Pi-pi interactions are non-covalent forces between aromatic rings.
Purpose of the Study:
- To investigate the role and stability of pi-pi interactions in protein structures.
- To analyze the thermodynamic relevance of different types of pi-pi interactions.
Main Methods:
- Utilized a database of 6166 experimental protein structures from the Protein Data Bank.
- Calculated 2-D potentials of mean force to determine the stability of residue pairs.
- Analyzed interactions between planar residues: Phenylalanine (Phe), Tyrosine (Tyr), Histidine (His), Arginine (Arg), Glutamic acid (Glu), and Aspartic acid (Asp).
Main Results:
- Identified and quantified the stability of aromatic-aromatic, aromatic-cation, and aromatic-anion pairs.
- Demonstrated the thermodynamic relevance of stacked complexes in proteins.
- Revealed the ubiquitous nature of these interactions across various protein structures.
Conclusions:
- Pi-pi interactions, particularly stacked complexes, are a significant stabilizing factor in protein architecture.
- These interactions play a crucial role in determining the overall stability and function of proteins.
- The findings highlight the importance of considering pi-pi interactions in protein design and drug discovery.
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