Submitted to: American Chemical Society Abstracts
Publication Type: Abstract only
Publication Acceptance Date: 9/1/2004
Publication Date: 10/20/2004
Citation: Kim, S. 2004. Investigation of cross-linking mechanism of proteins with frap technique[abstract]. American Chemical Society Abstracts. p.74 Interpretive Summary:
Technical Abstract: The FRAP (Fluorescence Recovery After Photobleaching) technique was introduced in 1974 to measure translational diffusion in a plasma membrane of single cells. Soon after, the method was improved, varied and extended and widely applied in studies of membrane dynamics. As this technique allows us to measure the self diffusion of macromolecules, their hydrodynamic radii can be deduced by using Stokes-Einstein relationship. This fact implies that the FRAP technique can serve as an effective tool for the investigation of the dynamics of biopolymers such as proteins and carbohydrates. A modified version of FRAP instrument was developed and constructed for the investigation of molecular dynamics of proteins and carbohydrates in various conditions. In this presentation, the principle of FRAP technique and its application to the investigation of the cross-linking mechanism of globular proteins will be discussed. For the cross-linking reaction, a mild reagent pair, EDC (1-[3-dimethylaminopropyl]-3-ethyl-carbodiimide hydrochloride) and NHS (N-hydroxysuccinimide), was employed.