Related Experiment Video
Updated: Jun 22, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
Published on: September 2, 2019
A tubular biocontainer: metal ion-induced 1D assembly of a molecularly engineered chaperonin
Shuvendu Biswas1, Kazushi Kinbara, Nobuhiro Oya
1Department of Chemistry and Biotechnology, School of Engineering and Center for NanoBio Integration, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
Abstract:
GroEL(SP/MC), prepared by genetic and chemical modifications of group I chaperonin protein GroEL, site-specifically possesses approximately 28 photochromic (spiropyran [SP] and merocyanine [MC]) units in the entrance parts of its cavity. Addition of divalent metal ions such as Mg(2+) to a tris-HCl buffer solution of GroEL(SP/MC) results in one-dimensional (1D) assembly of GroEL(SP/MC), affording cylindrical hollow fibers with a very large aspect ratio; the longest fiber was approximately 2.5 microm long, corresponding to a 170-mer of GroEL(SP/MC) (MW approximately 1.4 x 10(8)). When such long fibers are mixed with EDTA, they are cut into short-chain oligomers and eventually into monomeric GroEL(SP/MC). Similar to GroEL, GroEL(SP/MC) possesses a large binding affinity toward denatured proteins. When GroEL(SP/MC) undergoes 1D assembly after incubation with a denatured protein, guest-containing cylindrical fibers result.
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Structure of Porins
Bacterial Protein Maturation

