Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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

Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

Protein Folding

Protein Folding

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

BioMatics 1.0: A Wasserstein Distance Approach for Next-Generation Multiple Sequence Alignment.

Proteins·2026

Same author

Extending the classical sequence-structure-function paradigm through protein dynamics and context-dependent behavior.

FEBS letters·2026

Same author

IMMUND: A Diagnostic and Therapeutic Pipeline to Uncover the Convergence in Functional Perturbation at Early Stages of Neurodegenerative Diseases and Multiple Sclerosis Based on Protein Markers.

International journal of molecular sciences·2026

Same author

Intrinsic Disorder Status in Human Proteins Interacting With SARS-CoV-2 Proteins: Insights From Five Years of Translational Research.

Journal of cellular biochemistry·2026

Same author

Amyloid-β, Tau Protein, α-Synuclein, TDP-43, and FUS in Mixed Pathology: And Intrinsic Disorder to Rule Them All.

International journal of molecular sciences·2026

Same author

The role of tumor-infiltrating B cells in the development and pathogenesis of head and neck cancers: Implications for therapeutic approach.

International reviews of immunology·2026

Search research articles

Related Experiment Video

Updated: Jan 16, 2026

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

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

Published on: November 1, 2024

Conditional disorder in proteins: functional transitions between order and disorder.

Bhaswati Devi¹, Niharika Nag², Vladimir N Uversky³

¹Molecular and Structural Biophysics Laboratory, Department of Zoology, School of Life Sciences, North-Eastern Hill University, Shillong 793022, India. timir.tripathi@gmail.com.

Chemical Communications (Cambridge, England)

|October 2, 2025

Summary

Conditionally disordered proteins (CDPs) dynamically switch between ordered and disordered states, enabling crucial cellular roles. Understanding this conditional disorder is key to advancing structural biology and disease research.

More Related Videos

Optogenetic Phase Transition of TDP-43 in Spinal Motor Neurons of Zebrafish Larvae

Optogenetic Phase Transition of TDP-43 in Spinal Motor Neurons of Zebrafish Larvae

Published on: February 25, 2022

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

Published on: September 23, 2021

Related Experiment Videos

Last Updated: Jan 16, 2026

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

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

Published on: November 1, 2024

Optogenetic Phase Transition of TDP-43 in Spinal Motor Neurons of Zebrafish Larvae

Optogenetic Phase Transition of TDP-43 in Spinal Motor Neurons of Zebrafish Larvae

Published on: February 25, 2022

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

Published on: September 23, 2021

Area of Science:

Structural Biology
Biochemistry
Molecular Biology

Background:

The traditional view of proteins relies on static, ordered structures.
Emerging evidence highlights intrinsically disordered proteins (IDPs) and their dynamic nature.
Conditionally disordered proteins (CDPs) are a subset of IDPs that change conformation in response to stimuli.

Purpose of the Study:

To review the diverse landscape of conditional disorder in proteins.
To explore the functional significance of disorder-to-order transitions.
To discuss implications for cellular plasticity, disease, and therapeutic strategies.

Main Methods:

Literature review of conditional disorder.
Analysis of various CDP types (cryptic regions, redox-sensitive motifs, metamorphic proteins).
Examination of order-disorder-new order transitions.

Main Results:

CDPs exhibit dynamic transitions (e.g., redox, PTMs, ligand binding) enabling regulatory and signaling roles.
Conditional disorder is a conserved, functionally relevant feature across proteomes.
These transitions are crucial for cellular adaptability and response to stress.

Conclusions:

Conditional disorder expands the understanding of protein versatility beyond static structures.
CDP conformational heterogeneity presents challenges and opportunities for drug design.
Future research requires integrated biophysical and computational approaches to map and target CDPs.