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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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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...
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Intrinsically Disordered Proteins02:18

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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins07:24

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A protocol for the application of paramagnetic relaxation enhancement NMR spectroscopy to detect weak and transient inter- and intra-molecular interactions in intrinsically disordered proteins is presented.
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins12:47

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

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We describe here a method to identify multiple phosphorylations of an intrinsically disordered protein by Nuclear Magnetic Resonance Spectroscopy (NMR), using Tau protein as a case study. Recombinant Tau is isotopically enriched and modified in vitro by a kinase prior to data acquisition and...
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Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis07:54

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

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This protocol combines the characterization of a protein sample by capillary gel electrophoresis and a fast-binding screening for charged ligands by affinity capillary electrophoresis. It is recommended for proteins with a flexible structure, such as intrinsically disordered proteins, to determine any differences in binding for different...
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Estimation of Structural Sensitivity of Intrinsically Disordered Regions in Response to Hyperosmotic Stress in Living Cells Using FRET05:13

Estimation of Structural Sensitivity of Intrinsically Disordered Regions in Response to Hyperosmotic Stress in Living Cells Using FRET

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Intrinsically disordered regions (IDRs) are flexible protein domains that modify their conformation in response to environmental changes. Ensemble fluorescence resonance energy transfer (FRET) can estimate protein dimensions under different conditions. We present a FRET approach to assess IDR structural sensitivity in living Saccharomyces cerevisiae cells under hyperosmotic...
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Updated: Jan 19, 2026

Factors Affecting Intrinsically Disordered Proteins
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Intrinsically disordered proteins and phenotypic switching: Implications in cancer.

Vivek Kulkarni1, Prakash Kulkarni2

  • 1Division of Biology & Biological Engineering, California Institute of Technology, Pasadena, CA, United States.

Progress in Molecular Biology and Translational Science
|September 16, 2019
PubMed
Summary

Intrinsically disordered proteins (IDPs) influence cell behavior and disease. Their dynamic nature, or "conformational noise," may drive phenotypic switching in cancer through non-genetic pathways.

Keywords:
Conformational dynamicsNoiseOscillatory dynamicsProstate cancerProstate-associated gene 4State/phenotypic switching

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

Published on: September 23, 2021

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cancer Research

Background:

  • Intrinsically disordered proteins (IDPs) are abundant and crucial for biological processes like phenotypic switching.
  • Aberrant IDP interactions are linked to pathological conditions, including cancer.
  • Phenotypic switching in cancer is traditionally viewed as genetically determined.

Purpose of the Study:

  • To explore the role of intrinsically disordered protein (IDP) conformational dynamics in phenotypic switching.
  • To investigate the contribution of IDP conformational noise to non-genetic mechanisms in cancer.

Main Methods:

  • Review of existing literature on IDPs and cancer.
  • Analysis of IDP conformational dynamics and their impact on cellular phenotypes.
  • Discussion of cancer as a model system for studying IDP functions.

Main Results:

  • IDPs play significant roles in various biological processes, including phenotypic switching.
  • Conformational dynamics and noise of IDPs can modulate phenotypic switching.
  • Non-genetic mechanisms, influenced by IDP conformational noise, may contribute to phenotypic switching in cancer.

Conclusions:

  • Phenotypic switching in cancer may not be solely deterministic or genetically driven.
  • IDP conformational noise represents a significant factor in non-genetic phenotypic switching.
  • Understanding IDP dynamics is crucial for comprehending cancer heterogeneity and progression.