Michael Diehl Assistant Professor Departments of Bioengineering and Chemistry Rice University
	Probing Multi-Protein Dynamics with Single-Molecule Sensitivity
	The cellular mechanics of linear biomotor proteins often involves the cooperation of teams of motor proteins in the form of architecturally rich assemblies. Functioning in multiunit groups provides a means to regulate and enhance transport despite the stochastic behavior exhibited by single motor elements. Here, we explore such effects through the engineering of multi-biomotor protein assemblies, where the molecular properties of the assembly are precisely controlled. Our approach involves the design and synthesis of polymeric scaffolds that can be used as a backbone to assemble motors. Polymers are synthesized through the in vivo expression of artificial proteins. This method provides a genetic level control over macromolecular architecture, and consequently, discrete control over number of coupled motors, intermotor distance as well as the nature of the elastic interconnects between motors. We find the organizing multiple motor proteins along a single backbone results in a dramatic enhancement of both the backbone results in a dramatic enhancement of both the maximal ATP hydrolysis rate and the motor-complex velocity. Furthermore, coupling several proteins together removes the strain dependence of the velocity dependent step at zero load. These results demonstrate that our molecular handles over biomotor communicaiton can be used to tune the local correlations between motors and to redirect the dynamical properties of an assembly. In this wey, the materials approach adopted here can provide a novel means to deconvolve the molecular details that link the properties and function of multiprotein assemblies.
	Thursday, September 7, 2006 2:00 p.m. - Duncan Hall 3092 Rice University

ECE Affiliates Meeting

Last modified: August 10, 2006