title: A single-molecule dissection of ligand binding to a protein with intrinsic dynamics.
abstract: Protein dynamics have been suggested to have a crucial role in biomolecular recognition, but the precise molecular mechanisms remain unclear. Herein, we performed single-molecule fluorescence resonance energy transfer measurements for wild-type maltose-binding protein (MBP) and its variants to demonstrate the interplay of conformational dynamics and molecular recognition. Kinetic analysis provided direct evidence that MBP recognizes a ligand through an 'induced-fit' mechanism, not through the generally proposed selection mechanism for proteins with conformational dynamics such as MBP. Our results indicated that the mere presence of intrinsic dynamics is insufficient for a 'selection' mechanism. An energetic analysis of ligand binding implicated the critical role of conformational dynamics in facilitating a structural change that occurs upon ligand binding.
authors.affiliation: Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, Korea.
authors.forename: Eunkyung
authors.initials: E
authors.lastname: Kim
authors.forename: Sanghwa
authors.initials: S
authors.lastname: Lee
authors.forename: Aram
authors.initials: A
authors.lastname: Jeon
authors.forename: Jung Min
authors.initials: JM
authors.lastname: Choi
authors.forename: Hee-Seung
authors.initials: HS
authors.lastname: Lee
authors.forename: Sungchul
authors.initials: S
authors.lastname: Hohng
authors.forename: Hak-Sung
authors.initials: HS
authors.lastname: Kim
mesh_terms: D001665:Binding Sites; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D031541:Fluorescence Resonance Energy Transfer; D007700:Kinetics; D008024:Ligands; D058619:Maltose-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation
chemical_list: D029968:Escherichia coli Proteins; D008024:Ligands; D058619:Maltose-Binding Proteins