October 9 - 12, 2012
Building 10 & Natcher Conference Center
- General Schedule of Events
- Opening Plenary Session
- Concurrent Symposia Sessions
- Poster Sessions
- National Graduate Student Research Conference
- FARE Award Ceremony
- Special Exhibits on Resources for Intramural Research
- TSA Research Festival Exhibit Show
- Clinical Center Tours
- Research Festival Committees
- Past Research Festivals
A new TIRF single molecule calibration
| Thursday, November 07, 2013 — Poster Session II | |||
|---|---|---|---|
12:00 p.m. – 2:00 p.m. |
FAES Academic Center (Upper-Level Terrace) |
NINDS |
BIOENG-21 |
Author
- A. Popescu-Hategan
Abstract
A new total internal reflection fluorescence (TIRF) molecular calibration based on single molecule fluorescence is presented. Used to study myosin polymerization, it determined the number of molecules in each single filament formed in the presence or absence of a copolymerizing protein. Exchange and depolymerization were observed live in single filaments and their rates measured: first experimental evidence that exchange takes place by monomer addition as determined by single molecule calibration. Live observation of fibrin polymerization in TIRF was translated by this calibration in molecular information on the growth kinetics of fibers. Fibrin fibers thickened in time to thousands of molecules across, whereas some fibers reached early a stationary state. Diameters of fibers were calculated from this data and their evolution observed during growth to go up to hundreds of nm. This new approach in protein polymerization bridges the gap between molecular and assembled structure by determining macroscopic features of the polymer starting from single molecule observation thus providing information important for understanding the early events of polymerization.
