title: Artificial allosteric control of maltose binding protein.
abstract: We demonstrate the allosteric control of a protein based on mechanical tension. When substrate binding is accompanied by a significant change of conformation of the protein, a mechanical tension favoring one or the other conformation will alter the binding affinity for the substrate. We have constructed a chimera where the two lobes of the maltose-binding protein are covalently coupled to the ends of a DNA oligomer. The mechanical tension on the protein is controlled externally by exploiting the difference in stiffness between single stranded and double stranded DNA. We report that the binding affinity of the protein for its substrates is significantly altered by the tension.
authors.affiliation: Department of Physics and Astronomy, University of California-Los Angeles, Los Angeles, California 90095-1547, USA.
authors.forename: Brian
authors.initials: B
authors.lastname: Choi
authors.forename: Giovanni
authors.initials: G
authors.lastname: Zocchi
authors.forename: Stephen
authors.initials: S
authors.lastname: Canale
authors.forename: Yim
authors.initials: Y
authors.lastname: Wu
authors.forename: Sum
authors.initials: S
authors.lastname: Chan
authors.forename: L Jeanne
authors.initials: LJ
authors.lastname: Perry
mesh_terms: D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D004247:DNA / Q000737:chemistry* / Q000648:ultrastructure*; D007536:Isomerism; D007700:Kinetics; D058619:Maltose-Binding Proteins; D011485:Protein Binding; D011487:Protein Conformation; D013314:Stress, Mechanical; D013329:Structure-Activity Relationship
chemical_list: D002352:Carrier Proteins; D058619:Maltose-Binding Proteins; D004247:DNA