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Related Concept Videos

Protein Folding01:25

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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Protein Folding01:22

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Protein Folding01:22

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Molecular Chaperones and Protein Folding03:00

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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...
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Molecular Chaperones and Protein Folding03:00

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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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Related Experiment Video

Updated: Apr 18, 2026

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Protein folding. Phosphorylation regulates IDP folding.

Katharine H Wrighton

    Nature Reviews. Molecular Cell Biology
    |January 22, 2015
    PubMed
    Summary

    Phosphorylation controls how the intrinsically disordered protein 4E-BP2 folds, which determines its biological function. This finding offers new insights into protein regulation.

    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Protein Science

    Background:

    • Intrinsically disordered proteins (IDPs) lack stable structures but are crucial for cellular processes.
    • 4E-BP2 is an IDP involved in regulating protein synthesis.
    • Post-translational modifications, like phosphorylation, are known to affect protein function.

    Purpose of the Study:

    • To investigate the role of phosphorylation in regulating the structure and function of the intrinsically disordered protein 4E-BP2.

    Main Methods:

    • Utilized biochemical assays to study protein folding.
    • Employed phosphorylation techniques to modify 4E-BP2.
    • Assessed changes in protein function post-modification.

    Main Results:

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    Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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    • Demonstrated that phosphorylation directly influences the folding of 4E-BP2.
    • Showed a correlation between altered folding and changes in 4E-BP2's biological activity.
    • Identified specific phosphorylation sites impacting protein conformation.

    Conclusions:

    • Phosphorylation is a key regulatory mechanism for the intrinsically disordered protein 4E-BP2.
    • Modulating 4E-BP2 folding via phosphorylation is critical for its biological function.
    • Findings contribute to understanding IDP regulation in cellular pathways.