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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 Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Protein Folding

Protein Folding

Protein Folding

Protein Folding

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...

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Updated: Mar 22, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Predicting Conformational Disorder.

Philippe Lieutaud^1,2, François Ferron^1,2, Sonia Longhi^3,4

¹AFMB UMR 7257, Aix-Marseille Université, 163, avenue de Luminy, Case 932, 13288, Marseille Cedex 09, France.

Methods in Molecular Biology (Clifton, N.J.)

|April 27, 2016

Summary

This summary is machine-generated.

Intrinsically disordered proteins lack stable structures but perform vital functions. Identifying these disordered regions aids protein annotation and crystallization, focusing on prediction methods and induced folding.

Keywords:

Disorder databases and metaservers Induced folding Intrinsic disorder Intrinsically disordered proteins Intrinsically disordered regions Prediction methods

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Last Updated: Mar 22, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Area of Science:

Biochemistry
Structural Biology
Proteomics

Background:

A significant portion of proteins are intrinsically disordered, lacking a fixed 3D structure.
These proteins are crucial for various biological functions despite their conformational flexibility.
Disordered regions are recognized through sequence properties, enabling functional annotation.

Purpose of the Study:

To review current methodologies for predicting intrinsically disordered protein regions.
To identify regions within proteins that undergo induced folding.

Main Methods:

Analysis of amino acid sequence properties to identify disorder.
Computational methods for predicting protein disorder.
Characterization of regions involved in disorder-to-order transitions.

Main Results:

Disordered regions can be identified based on sequence characteristics.
Predictive models are available for identifying intrinsically disordered regions.
Understanding induced folding is key to functional annotation.

Conclusions:

Predicting protein disorder is essential for functional annotation and domain boundary delineation.
Methods for identifying disordered regions are crucial for structural biology and drug discovery.
Further research into induced folding mechanisms is warranted.