Chemical double-mutant cycles: dissecting non-covalent interactions.
Thermodynamic double-mutant cycles and triple-mutant boxes are widely employed for the experimental quantification of non-covalent interactions and cooperative effects in proteins. This review describes the application of these powerful methodologies to the study of non-covalent interactions in synthetic systems.
Cockroft
Scott L
SL
Centre for Chemical Biology, Department of Chemistry, Krebs Institute for Biomolecular Science, University of Sheffield, S3 7HF, UK.
Hunter
Christopher A
CA
D000596:Amino Acids / Q000737:chemistry; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*; D055672:Static Electricity; D013816:Thermodynamics
D000596:Amino Acids; D011506:Proteins