Specific Interaction Between GroEL and Denatured Protein Measured by Compression-free Force Spectroscopy

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 2003 Jun 28

PMID 12829503

Citations 8

Authors

Hiroshi Sekiguchi

Hideo Arakawa

Hideki Taguchi

Takeshi Ito

Ryohei Kokawa

Atsushi Ikai

Affiliations

Soon will be listed here.

Abstract

We investigated the interaction between GroEL and a denatured protein from a mechanical point of view using an atomic force microscope. Pepsin was bound to an atomic force microscope probe and used at a neutral pH as an example of denatured proteins. To measure a specific and delicate interaction force, we obtained force curves without pressing the probe onto GroEL molecules spread on a mica surface. Approximately 40 pN of tensile force was observed for approximately 10 nm while pepsin was pulled away from the chaperonin after a brief contact. This length of force duration corresponding to the circumference of GroEL's interior cavity was shortened by the addition of ATP. The relation between the observed mechanical parameters and the chaperonin's refolding function is discussed.

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