Allosteric control through mechanical tension.
Conformational changes of proteins modulate their function. In allosteric control, the conformational change is induced by the binding of a signaling molecule. Here we insert a "molecular spring" on the enzyme guanylate kinase, to control the conformation of this protein. The stiffness of the spring can be varied externally, which allows one to exert a controlled mechanical tension between the two points on the protein's surface where the spring is attached. We show that by applying and releasing the tension we can reversibly turn the enzyme off and on.
Choi
Brian
B
Department of Physics and Astronomy, University of California Los Angeles, 90095-1547, USA.
Zocchi
Giovanni
G
Wu
Yim
Y
Chan
Sum
S
Jeanne Perry
L
L
D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D051528:Guanylate Kinases; D007700:Kinetics; D058619:Maltose-Binding Proteins; D008956:Models, Chemical; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009703:Nucleoside-Phosphate Kinase / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D002352:Carrier Proteins; D058619:Maltose-Binding Proteins; D004247:DNA; D009703:Nucleoside-Phosphate Kinase; D051528:Guanylate Kinases