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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

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...

Structural Protein Function

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...

The Equilibrium Binding Constant and Binding Strength

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

Protein and Protein Structures

Protein and Protein Structures

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Related Experiment Video

Updated: Feb 12, 2026

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis

Published on: June 20, 2025

Structural Ensemble Modulation upon Small-Molecule Binding to Disordered Proteins.

Gabriella T Heller¹, Massimiliano Bonomi¹, Michele Vendruscolo¹

¹Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.

Journal of Molecular Biology

|March 30, 2018

Summary

This summary is machine-generated.

Small molecules can target intrinsically disordered proteins (IDPs), which are implicated in diseases. A "structural ensemble modulation" framework helps clarify concepts for developing new therapies against these challenging targets.

Keywords:

disordered proteins drug discovery entropy small molecules structural ensembles

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Area of Science:

Biochemistry and Structural Biology
Drug Discovery and Medicinal Chemistry

Background:

Growing interest in targeting intrinsically disordered proteins (IDPs) with small molecules for clinical applications.
Small-molecule binding to IDPs is considered unorthodox, yet examples are increasingly reported.
Existing models for IDP-small molecule interactions are varied and sometimes contradictory.

Purpose of the Study:

To introduce a unifying "structural ensemble modulation" framework.
To clarify terminology and organize concepts in the field of IDP-small molecule interactions.
To facilitate comparison between different studies and promote understanding of underlying principles.

Main Methods:

Conceptual framework development.
Literature review and synthesis of existing models.
Analysis of reported examples of small-molecule binding to IDPs.

Main Results:

Proposal of the "structural ensemble modulation" view as a unifying concept.
Demonstration of how this framework can reconcile apparently contradictory observations.
Identification of key principles governing IDP-small molecule interactions.

Conclusions:

The "structural ensemble modulation" framework provides a clearer perspective on targeting IDPs.
This understanding is crucial for the rational design of novel therapeutic compounds.
Targeting IDPs holds promise for treating a wide range of human diseases.