Protein conformational dynamics dictate the binding affinity for a ligand.
Interactions between a protein and a ligand are essential to all biological processes. Binding and dissociation are the two fundamental steps of ligand-protein interactions, and determine the binding affinity. Intrinsic conformational dynamics of proteins have been suggested to play crucial roles in ligand binding and dissociation. Here, we demonstrate how protein dynamics dictate the binding and dissociation of a ligand through a single-molecule kinetic analysis for a series of maltose-binding protein mutants that have different intrinsic conformational dynamics and dissociation constants for maltose. Our results provide direct evidence that the ligand dissociation is determined by the intrinsic opening rate of the protein.
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea.
Moon-Hyeong
MH
Seo
Department of Physics and Astronomy, Seoul National University, Seoul 151-747, Korea.
Jeongbin
J
Park
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea.
Eunkyung
E
Kim
1] Department of Physics and Astronomy, Seoul National University, Seoul 151-747, Korea [2] Department of Biophysics and Chemical Biology, Seoul National University, Seoul 151-747, Korea [3] National Center for Creative Research Initiatives, Seoul National University, Seoul 151-747, Korea.
Sungchul
S
Hohng
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea.
Hak-Sung
HS
Kim
D008024:Ligands; D058619:Maltose-Binding Proteins / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation
D008024:Ligands; D058619:Maltose-Binding Proteins