Ligand effects on protein thermodynamic stability.
A simple, partition-function formalism is used to describe the coupling between ligand binding and protein equilibrium unfolding. This general theoretical framework is shown to provide an adequate basis for the analysis of experimental ligand effects on the unfolding of complex protein systems. Nevertheless, the most important consequences of ligand binding for protein thermodynamic stability, as exposed by the partition-function approach, are found to be those demonstrated by Julian Sturtevant about 20 years ago.
Sanchez-Ruiz
Jose M
JM
Departamento de Quimica Fisica, Campus Fuentenueva s/n, Universidad de Granada, 18071-Granada, Spain. sanchezr@ugr.es
D006801:Humans; D008024:Ligands; D010649:Phenylalanine / Q000737:chemistry; D010651:Phenylalanine Hydroxylase / Q000737:chemistry; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D008024:Ligands; D011506:Proteins; D010649:Phenylalanine; D010651:Phenylalanine Hydroxylase