Related Experiment Video
Updated: May 9, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
Published on: December 17, 2016
Hidden order in the GroEL-GroES-(ADP)7 chaperonin: forms, folding, and ADP-binding sites
1Institute for Theoretical Physics, University of Nijmegen, Toernooiveld, Nijmegen, The Netherlands. alo@sci.kun.nl
Abstract:
A molecular crystallography approach reveals the existence of a hidden order in GroEL-GroES-(ADP)(7). The new crystallographic symmetry concepts required are first illustrated for a hypothetical planar molecule. Their application to the chaperonin complex leads to molecular forms with vertices having integral coordinates (the indices) with respect to a symmetry-adapted basis and to folding points approximated by ideal C(alpha) positions with rational indices connected by integral scale-rotations, just as for the vertices of the molecular forms. The Mg(+2)-ions at nucleotide binding sites are symmetry-related in a similar way to C(alpha)'s folding points.
More Related Videos
08:58In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
Published on: September 2, 2019
13:35Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
Published on: May 23, 2025
Related Concept Videos
Protein Folding
Protein Folding
Molecular Chaperones and Protein Folding
The...
ATP Synthase: Structure
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Molecular Chaperones and Protein Folding
The...