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

Fingerprint

Peptides
Spectroscopy
Rate constants
Chemical activation
Proteins
Kinetics

All Science Journal Classification (ASJC) codes

  • Engineering(all)

Cite this

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.

The characteristic analysis of the specific interaction between PDZ-domain and its recognition peptide by dynamic force spectroscopy. / Maki, Tei; Kidoaki, Satoru; Matsuda, Takehisa; Usui, Kengo; Suzuki, Harukazu; Ito, Masayoshi; Hayashizaki, Yoshihide.

2005. 3231-3232 Paper presented at 54th SPSJ Symposium on Macromolecules, Yamagata, Japan.

Research output: Contribution to conferencePaper

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' Paper presented at 54th SPSJ Symposium on Macromolecules, Yamagata, Japan, 9/20/05 - 9/22/05, pp. 3231-3232.
Maki T, Kidoaki S, Matsuda T, Usui K, Suzuki H, Ito M et al. The characteristic analysis of the specific interaction between PDZ-domain and its recognition peptide by dynamic force spectroscopy. 2005. Paper presented at 54th SPSJ Symposium on Macromolecules, Yamagata, Japan.
Maki, Tei ; Kidoaki, Satoru ; Matsuda, Takehisa ; Usui, Kengo ; Suzuki, Harukazu ; Ito, Masayoshi ; Hayashizaki, Yoshihide. / The characteristic analysis of the specific interaction between PDZ-domain and its recognition peptide by dynamic force spectroscopy. Paper presented at 54th SPSJ Symposium on Macromolecules, Yamagata, Japan.2 p.
@conference{bd0b72dfae5348d2be6b6e86051a0077,
title = "The characteristic analysis of the specific interaction between PDZ-domain and its recognition peptide by dynamic force spectroscopy",
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.",
author = "Tei Maki and Satoru Kidoaki and Takehisa Matsuda and Kengo Usui and Harukazu Suzuki and Masayoshi Ito and Yoshihide Hayashizaki",
year = "2005",
month = "12",
day = "1",
language = "English",
pages = "3231--3232",
note = "54th SPSJ Symposium on Macromolecules ; Conference date: 20-09-2005 Through 22-09-2005",

}

TY - CONF

T1 - The characteristic analysis of the specific interaction between PDZ-domain and its recognition peptide by dynamic force spectroscopy

AU - Maki, Tei

AU - Kidoaki, Satoru

AU - Matsuda, Takehisa

AU - Usui, Kengo

AU - Suzuki, Harukazu

AU - Ito, Masayoshi

AU - Hayashizaki, Yoshihide

PY - 2005/12/1

Y1 - 2005/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=33645571915&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33645571915&partnerID=8YFLogxK

M3 - Paper

AN - SCOPUS:33645571915

SP - 3231

EP - 3232

ER -