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Related Concept Videos

Protein Folding01:25

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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.
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When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
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Related Experiment Video

Updated: Jul 19, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Protein folding and wring resonances.

J Bohr1, H Bohr, S Brunak

  • 1Physics Department, Building 307, The Technical University of Denmark, DK-2800 Lyngby, Denmark. jakob.bohr@fysik.dtu.dk

Biophysical Chemistry
|January 31, 1997
PubMed
Summary

Protein chains exhibit topological constraints, leading to wring modes that can resonate within cells. These wring modes are proposed to drive protein folding and denaturation, explaining both cold and hot unfolding phenomena.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Dynamics

Background:

  • Proteins fold into complex three-dimensional structures essential for their function.
  • The dynamics and conformational changes of proteins are critical to cellular processes.
  • Understanding protein folding and unfolding mechanisms remains a central challenge in molecular biology.

Purpose of the Study:

  • To investigate the role of topological constraints in protein dynamics.
  • To propose a novel mechanism for protein folding and denaturation based on 'wring modes'.
  • To explore the resonance between protein wring modes and cellular molecular modes.

Main Methods:

  • Theoretical analysis of polypeptide chain topology.
  • Modeling of protein backbone excitations as 'wring modes'.
  • Investigation of conditions for structural transformations (folding/unfolding).

Main Results:

  • Protein polypeptide chains exhibit topological constraints leading to long-range 'wring modes'.
  • Specific protein lengths allow wring modes to resonate with cellular molecular modes.
  • Protein folding is proposed to occur when wring excitation amplitude favors backbone bending.
  • Both cold and hot denaturation are explained as consequences of the wring mode model.
  • Native proteins possess an intrinsic standing wring mode.

Conclusions:

  • Wring modes represent a fundamental aspect of protein dynamics and conformational changes.
  • The proposed model provides a unified explanation for protein folding, denaturation, and cellular resonance.
  • This framework offers new insights into the physical principles governing protein structure and function.