Sub-Diffraction Temperature Mapping of Protein Interconversions
Abstract
Currently, spatially resolved temperature mapping of intracellular proteins is difficult to achieve using available imaging methods. The objective this effort is to enable sub-diffraction temperature mapping to quantify free energies of interconverting or interacting proteins. In other words study the microscopic thermodynamic action of protein size molecules associated with human performance, tissue regeneration, or even wound healing. Furthermore, limitations in spatial resolution hinder the ability to quantify free energies as proteins interconvert among conformations within the cellular milieu. The offeror proposes then, that thermal expansion differences in a so called multi-material nano-antenna will result in lattice mismatches, altering the plasmonic resonance (the charged species resonance). To overcome the diffraction limit of particle size, polarized excitation will be used to optically isolate subsets of nano-antennas. High-resolution temperature maps will be reconstructed from the center points of optically resolved nano-antennas and, finally, parallel imaging of temperature maps and labeled proteins will be conducted to quantify the free energies of thermodynamics associated with proteins.
Document Details
- Document Type
- DoD Grant Award
- Publication Date
- Jul 15, 2016
- Source ID
- FA95501610272
Entities
People
- Somin Eunice Lee
Organizations
- Air Force Office of Scientific Research
- United States Air Force
- University of Michigan