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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
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The chair conformation is the most stable form of cyclohexane due to the absence of angle and torsional strain. The absence of angle strain is a result of cyclohexane’s bond angle being very close to the ideal tetrahedral bond angle of 109.5° in its chair conformer. Similarly, the torsional strain is also absent owing to the perfectly staggered arrangement of bonds.
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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.
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At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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Updated: Jan 9, 2026

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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Backbone conformational entropy change in helix folding.

Uroš Zavrtanik1, Jurij Lah1, San Hadži1

  • 1Department of Physical Chemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia.

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Summary

Researchers quantified the backbone conformational entropy change during alpha-helix formation using differential scanning calorimetry. This provides a more accurate understanding of protein folding thermodynamics and intrinsically disordered proteins.

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Area of Science:

  • Biophysics
  • Thermodynamics
  • Protein Folding

Background:

  • Protein folding is driven by thermodynamic forces, with conformational entropy loss being a major opposing factor.
  • Quantifying backbone conformational entropy (ΔSBB) in alpha-helix formation is experimentally challenging due to coupled processes.

Purpose of the Study:

  • To directly measure the backbone conformational entropy change accompanying alpha-helix formation.
  • To refine helix-coil parameters using a robust thermodynamic model.

Main Methods:

  • Utilized differential scanning calorimetry to measure absolute heat capacities of alanine peptides.
  • Employed an ensemble-based statistical-thermodynamic model with Bayesian inference.

Main Results:

  • Determined the backbone entropy change for the helix-to-coil transition to be ΔSBB = (5.2 ± 0.3) cal mol-1 K-1 per peptide unit.
  • Obtained a unified thermodynamic picture including enthalpy and heat capacity changes for alpha-helix formation.

Conclusions:

  • The measured ΔSBB aligns with recent molecular dynamics simulations, offering a more accurate experimental value.
  • Findings have significant implications for understanding protein folding energetics and intrinsically disordered proteins.