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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
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...

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Related Experiment Video

Updated: Jun 23, 2026

Kinematic History of a Salient-recess Junction Explored through a Combined Approach of Field Data and Analog Sandbox Modeling
06:55

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Published on: August 5, 2016

Exploiting the downhill folding regime via experiment.

Victor Muñoz, Mourad Sadqi, Athi N Naganathan

    HFSP Journal
    |May 14, 2009
    PubMed
    Summary

    New experimental tools now allow detailed studies of protein folding, including downhill folding proteins. This provides insights into folding barriers, cooperativity, and aids in refining computer simulations.

    Area of Science:

    • Biochemistry
    • Biophysics
    • Computational Biology

    Background:

    • Traditional protein folding studies focus on two-state kinetics and equilibrium constants.
    • Recent advances enable exploration of proteins folding in the downhill regime, with minimal or no free energy barriers.

    Purpose of the Study:

    • To detail new experimental approaches for studying protein folding.
    • To investigate downhill folding proteins and their accessible conformations.
    • To provide tools for estimating folding barriers and characterizing structural heterogeneity.

    Main Methods:

    • Utilizing free energy surface approaches combined with experimental techniques.
    • Measuring atomic-level structural heterogeneity in partially folded protein ensembles.
    • Determining dynamic modes driving protein folding processes.

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    Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
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    Published on: September 15, 2010

    High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
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    High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

    Published on: June 29, 2021

    Related Experiment Videos

    Last Updated: Jun 23, 2026

    Kinematic History of a Salient-recess Junction Explored through a Combined Approach of Field Data and Analog Sandbox Modeling
    06:55

    Kinematic History of a Salient-recess Junction Explored through a Combined Approach of Field Data and Analog Sandbox Modeling

    Published on: August 5, 2016

    Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
    10:50

    Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

    Published on: September 15, 2010

    High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
    04:37

    High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

    Published on: June 29, 2021

    Main Results:

    • Development of methods to estimate thermodynamic and kinetic folding barriers.
    • Availability of techniques to measure structural heterogeneity at atomic resolution.
    • Capability to determine dynamic folding modes and their evolution.

    Conclusions:

    • Experimental capabilities now allow detailed investigation of protein folding mechanisms, including downhill folding.
    • These advancements facilitate addressing fundamental questions on folding cooperativity and stability.
    • The high level of experimental detail serves as a benchmark for computational folding simulations and force-field development.