Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 22, Issue 2, Pages -Publisher
MDPI
DOI: 10.3390/ijms22020828
Keywords
coupling energy; site-directed mutagenesis; interaction networks
Funding
- Sapienza University of Rome [B52F16003410005, RP11715C34AEAC9B, RM1181641C2C24B9]
- Associazione Italiana per la Ricerca sul Cancro [24551]
- Istituto Pasteur Italia (Teresa Ariaudo Research Project 2018)
- Swedish Research Council [2020-04395]
- FIRC-AIRC fellowship
- Swedish Research Council [2020-04395] Funding Source: Swedish Research Council
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This article introduces a quantitative measurement method for intramolecular and intermolecular interactions in protein structure, focusing on the principles, applications, and considerations of double-mutant cycles analysis. Double mutant cycles can be a powerful tool to investigate allosteric mechanisms in protein binding reactions as well as elusive states in protein folding pathways.
Quantitative measurement of intramolecular and intermolecular interactions in protein structure is an elusive task, not easy to address experimentally. The phenomenon denoted 'energetic coupling' describes short- and long-range interactions between two residues in a protein system. A powerful method to identify and quantitatively characterize long-range interactions and allosteric networks in proteins or protein-ligand complexes is called double-mutant cycles analysis. In this review we describe the thermodynamic principles and basic equations that underlie the double mutant cycle methodology, its fields of application and latest employments, and caveats and pitfalls that the experimentalists must consider. In particular, we show how double mutant cycles can be a powerful tool to investigate allosteric mechanisms in protein binding reactions as well as elusive states in protein folding pathways.
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