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Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

Ligand Binding Sites

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

Metal-Ligand Bonds

Metal-Ligand Bonds

The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...

Ligand Binding and Linkage

Ligand Binding and Linkage

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...

Ligand Binding and Linkage

Ligand Binding and Linkage

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Related Experiment Video

Updated: Feb 2, 2026

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis

Published on: August 22, 2018

Targeting the Intrinsically Disordered Proteome Using Small-Molecule Ligands.

Sławomir Wójcik¹, Melissa Birol², Elizabeth Rhoades²

¹Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, United States; Department of Chemistry, Yale University, New Haven, CT, United States.

Methods in Enzymology

|November 26, 2018

Summary

This summary is machine-generated.

Intrinsically disordered proteins (IDPs) are key to many functions but hard to target. New methods leverage their flexibility and phase separation for small-molecule drug development and bioengineering.

Keywords:

Coacervation Drug design Intrinsically disordered proteins Protein aggregation Protein disorder Small-molecule design

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Related Experiment Videos

Last Updated: Feb 2, 2026

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis

Published on: August 22, 2018

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Area of Science:

Biochemistry and Molecular Biology
Drug Discovery and Development
Protein Science

Background:

Intrinsically disordered proteins (IDPs) and regions (IDRs) are prevalent in the proteome.
They play crucial roles in physiological and pathological processes.
Their lack of stable structure poses challenges for therapeutic targeting.

Purpose of the Study:

To review strategies for targeting IDPs using small molecules.
To explore how conformational flexibility and phase separation of IDPs can be exploited.
To discuss methods for characterizing IDPs and identifying therapeutic partners.

Main Methods:

Review of theoretical and experimental approaches for IDP characterization.
Focus on thermodynamic and single-molecule techniques.
Analysis of IDP conformational flexibility and phase separation properties.

Main Results:

IDPs' conformational flexibility and phase separation are amenable to small-molecule manipulation.
Novel techniques enable better characterization of IDPs.
These methods can identify partners that shift protein ensembles toward desired conformations.

Conclusions:

Small molecules can effectively target intrinsically disordered proteins.
Advanced characterization techniques are crucial for understanding and manipulating IDPs.
Exploiting IDP properties opens new avenues for drug development and bioengineering.