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Related Concept Videos

Protein Folding01:25

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 Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Intrinsically Disordered Proteins02:18

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 Proteins02:18

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...
Protein Organization01:13

Protein Organization

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Updated: Jun 7, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Evolution of structurally disordered proteins promotes neostructuralization.

Jessica Siltberg-Liberles

    Molecular Biology and Evolution
    |November 2, 2010
    PubMed
    Summary
    This summary is machine-generated.

    Structurally disordered regions in proteins evolve dynamically, with their extent and location varying across protein families. This flexibility impacts protein structural evolution and secondary structure propensities.

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    Related Experiment Videos

    Last Updated: Jun 7, 2026

    NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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    Published on: November 1, 2024

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    High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
    08:48

    High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

    Published on: April 28, 2022

    Area of Science:

    • Evolutionary biology
    • Structural bioinformatics
    • Molecular evolution

    Background:

    • Protein structure conservation typically exceeds sequence conservation.
    • Investigating the evolution of intrinsically disordered regions (IDRs) is crucial for understanding protein structural evolution.
    • Paralogs and orthologs provide insights into the evolutionary dynamics of protein families.

    Discussion:

    • The study examined evolutionary dynamics of structural disorder in protein families using phylogenetic analysis, disorder prediction, and secondary structure prediction.
    • Results indicate that the extent and location of disordered regions are not universally conserved.
    • High conformational flexibility in IDRs influences protein structural evolution and secondary structure propensities.

    Key Insights:

    • Disordered regions exhibit significant evolutionary plasticity in their location and extent.
    • Conformational flexibility of disordered regions plays a key role in shaping protein evolution.
    • Evolutionary changes in disordered regions can alter secondary structure propensities within homologous protein families.

    Outlook:

    • Further research can explore the functional implications of evolving disordered regions.
    • Investigating specific environmental influences on disordered region evolution is warranted.
    • Comparative studies across diverse protein families will deepen our understanding of protein structural evolution.