The characteristic analysis of the specific interaction between PDZ-domain and its recognition peptide by dynamic force spectroscopy

Tei Maki, Satoru Kidoaki, Takehisa Matsuda, Kengo Usui, Harukazu Suzuki, Masayoshi Ito, Yoshihide Hayashizaki

Research output: Contribution to conferencePaper

Abstract

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.

Original languageEnglish
Pages3231-3232
Number of pages2
Publication statusPublished - Dec 1 2005
Event54th SPSJ Symposium on Macromolecules - Yamagata, Japan
Duration: Sep 20 2005Sep 22 2005

Other

Other54th SPSJ Symposium on Macromolecules
CountryJapan
CityYamagata
Period9/20/059/22/05

All Science Journal Classification (ASJC) codes

  • Engineering(all)

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    Maki, T., Kidoaki, S., Matsuda, T., Usui, K., Suzuki, H., Ito, M., & Hayashizaki, Y. (2005). The characteristic analysis of the specific interaction between PDZ-domain and its recognition peptide by dynamic force spectroscopy. 3231-3232. Paper presented at 54th SPSJ Symposium on Macromolecules, Yamagata, Japan.