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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

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Related Experiment Video

Updated: Jun 26, 2026

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Published on: December 3, 2015

Linking folding and binding.

Peter E Wright¹, H Jane Dyson

¹Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States. wright@scripps.edu

Current Opinion in Structural Biology

|January 23, 2009

Summary

This summary is machine-generated.

Intrinsically disordered proteins fold upon target binding. Recent advances in biophysical techniques and computational methods offer new insights into their conformational dynamics and biological functions.

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Area of Science:

Biochemistry
Structural Biology
Molecular Biology

Background:

Many cellular proteins are intrinsically disordered, adopting specific structures only upon binding to targets.
Characterization of these proteins, both free and bound, has seen significant growth.
Understanding their dynamic nature is crucial for comprehending cellular processes.

Purpose of the Study:

To review recent advances in the study of intrinsically disordered proteins (IDPs).
To highlight new techniques for characterizing IDP conformational ensembles.
To explore progress in predicting recognition elements and understanding binding mechanisms.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy remains a key technique.
Emerging biophysical methods are increasingly used to define conformational ensembles.
Computational approaches aid in predicting recognition elements and binding kinetics.

Main Results:

New techniques provide detailed insights into the conformational states of IDPs.
Advances in understanding coupled folding-binding kinetics and mechanisms.
Post-translational modifications are shown to modulate IDP function.

Conclusions:

Recent research offers novel perspectives on IDP conformational propensities and interactions.
Emerging principles are beginning to explain the biological roles of IDPs.
Continued investigation promises deeper understanding of these dynamic molecules.