To characterize the specific interaction between PDZ-protein (TIP-1) and its recognition peptide (PDZ-pep), dynamic force spectroscopy (DPS) for these pair was performed using AFM. Unbinding forces of these pair were measured under different conditions of AFM tip retracting velocity. The unbinding force spectra on logarithmic force-loading rate exhibited two different rate regimes each of where the forces linearly increased with the logarithmic rate. Based on DFS theory, positions of two different activation barriers in reaction coordinate and dissociation rate constants in each barrier were evaluated from slopes and x-intercepts of the two linear regimes. Two-step dissociation kinetics between TIP-1 and PDZ-pep was suggested.
|Number of pages||2|
|Publication status||Published - Dec 1 2005|
|Event||54th SPSJ Symposium on Macromolecules - Yamagata, Japan|
Duration: Sep 20 2005 → Sep 22 2005
|Other||54th SPSJ Symposium on Macromolecules|
|Period||9/20/05 → 9/22/05|
All Science Journal Classification (ASJC) codes