Characterization of novel synthetic biomaterials for protein immobilization
EMSL Project ID
48243
Abstract
Our goal is to develop a mechanistic understanding of optimal material properties that would permit the functional stabilization of broad classes of proteins with utility to a range of detection and decontamination applications. Current approaches aimed at preserving enzyme function following immobilization on solid supports rely on trial-and-error protocols that do not address how material properties affect protein structure and dynamics, with the result that general principles have not been formulated to enable the deployment of enzyme catalysts to mediate the detection or decontamination of a range of contaminants. We propose to use advanced fluorescence spectroscopy and both solution and solid state NMR methods to measure how material properties affect catalytically important domain motions following protein immobilization, explicitly addressing how adsorption, chemical cross-linking, and protein tethering methods affect the structure, dynamics, and function of several well-characterized proteins. Protein domain motions will be measured using newly developed molecular probes that bindrigidly to the protein backbone that reflect domain motions. NMR spectroscopy will provide complementary information regarding smaller scale motions, i.e., protein secondary structure and side chain motions. Experimentally, measured domain motions and enzyme function will be directly compared with molecular dynamics simulations that explicitly take into account material properties and diffusion of substrates to active sites, thus providing a predictive understanding of the physical properties that need to be preserved in developing new materials for enzyme immobilization.
Project Details
Start Date
2014-01-22
End Date
2014-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Co-Investigator(s)
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