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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 Dynamics in Living Cells

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Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

Protein Folding

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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.
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Related Experiment Video

Updated: May 6, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

From protein sequence to dynamics and disorder with DynaMine.

Elisa Cilia¹, Rita Pancsa, Peter Tompa

¹1] MLG, Département d'Informatique, Université Libre de Bruxelles, Boulevard du Triomphe, CP 212, 1050 Brussels, Belgium [2] Interuniversity Institute of Bioinformatics in Brussels, ULB-VUB, La Plaine Campus, Triomflaan, BC building, 6th floor, CP 263, 1050 Brussels, Belgium.

Nature Communications

|November 15, 2013

Summary

DynaMine predicts protein backbone dynamics using only sequence information. This tool accurately identifies protein structural regions and disordered areas, aiding molecular biologists.

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Last Updated: May 6, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

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Published on: April 13, 2022

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

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

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

Published on: July 16, 2017

Area of Science:

Biophysics
Computational Biology
Structural Biology

Background:

Protein function is intrinsically linked to its dynamics, but obtaining accurate dynamics information is challenging.
Existing methods for predicting protein dynamics often require extensive experimental data or complex structural information.

Purpose of the Study:

To develop a fast and accurate predictor of protein backbone dynamics using only amino acid sequence.
To create a tool, DynaMine, capable of identifying different structural organizations and disordered regions within proteins.

Main Methods:

Assembled a dataset from experimental data of proteins in solution.
Quantified backbone dynamics properties at the amino-acid level.
Developed DynaMine, a sequence-based predictor for protein dynamics.

Main Results:

DynaMine accurately predicts protein backbone dynamics from sequence alone.
The predictor distinguishes various structural regions, including folded domains, disordered linkers, and binding motifs.
Identified disordered regions with accuracy comparable to sophisticated existing predictors, without prior disorder knowledge or 3D structure.

Conclusions:

DynaMine offers a valuable new method for molecular biologists to assess protein dynamics.
The tool demonstrates significant potential in characterizing protein structural and dynamical properties.
Applicable to diverse proteins, including human p53 and adenovirus E1A protein.