title: Force spectroscopy studies on protein-ligand interactions: a single protein mechanics perspective.
abstract: Protein-ligand interactions are ubiquitous and play important roles in almost every biological process. The direct elucidation of the thermodynamic, structural and functional consequences of protein-ligand interactions is thus of critical importance to decipher the mechanism underlying these biological processes. A toolbox containing a variety of powerful techniques has been developed to quantitatively study protein-ligand interactions in vitro as well as in living systems. The development of atomic force microscopy-based single molecule force spectroscopy techniques has expanded this toolbox and made it possible to directly probe the mechanical consequence of ligand binding on proteins. Many recent experiments have revealed how ligand binding affects the mechanical stability and mechanical unfolding dynamics of proteins, and provided mechanistic understanding on these effects. The enhancement effect of mechanical stability by ligand binding has been used to help tune the mechanical stability of proteins in a rational manner and develop novel functional binding assays for protein-ligand interactions. Single molecule force spectroscopy studies have started to shed new lights on the structural and functional consequence of ligand binding on proteins that bear force under their biological settings.
authors.affiliation: State Key Laboratory of Precision Measurements Technology and Instruments, School of Precision Instrument and Opto-Electronics Engineering, Tianjin University, Tianjin 300072, PR China.
authors.forename: Xiaotang
authors.initials: X
authors.lastname: Hu
authors.affiliation: State Key Laboratory of Precision Measurements Technology and Instruments, School of Precision Instrument and Opto-Electronics Engineering, Tianjin University, Tianjin 300072, PR China; Department of Chemistry, University of British Columbia, Vancouver, BC V6T 1Z1, Canada. Electronic address: Hongbin@chem.ubc.ca.
authors.forename: Hongbin
authors.initials: H
authors.lastname: Li
mesh_terms: D006801:Humans; D008024:Ligands; D055595:Mechanical Phenomena; D018625:Microscopy, Atomic Force / Q000379:methods*; D052898:Optical Tweezers; D011485:Protein Binding; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D013057:Spectrum Analysis / Q000379:methods*
chemical_list: D008024:Ligands; D011506:Proteins
keywords: Binding assay; Force spectroscopy; Mechanical stability; Protein unfolding; Protein–ligand interaction