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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

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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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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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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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The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
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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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Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
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Molecular Fluctuations as a Ruler of Force-Induced Protein Conformations.

Andrew Stannard1, Marc Mora1, Amy E M Beedle1

  • 1Department of Physics, Randall Centre for Cell and Molecular Biophysics and London Centre for Nanotechnology, King's College London, Strand, WC2R 2LS London, United Kingdom.

Nano Letters
|March 25, 2021
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Summary
This summary is machine-generated.

Researchers measured protein fluctuations using magnetic tweezers to understand protein stiffness changes during unfolding and refolding. This reveals how proteins respond to mechanical force, crucial for mechanosensing.

Keywords:
energy landscapeprotein fluctuationsprotein foldingprotein nanomechanicsprotein stiffnesssingle molecule magnetic tweezers

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Area of Science:

  • Biophysics
  • Biochemistry
  • Polymer Physics

Background:

  • Molecular fluctuations reflect a protein's energy landscape and dynamics.
  • Variance analysis is key to studying protein dynamics, but measuring probe-independent fluctuations under mechanical force is challenging.
  • Steered molecular dynamics simulations are currently the primary method for this measurement.

Purpose of the Study:

  • To develop and apply a method for measuring probe-independent protein fluctuations under mechanical force.
  • To investigate changes in protein stiffness during unfolding and refolding transitions.
  • To understand the relationship between mechanical force, protein conformational changes, and polymer physics models.

Main Methods:

  • Utilized single-molecule magnetic tweezers to apply controlled forces to proteins.
  • Performed variance analysis on protein end-to-end fluctuations during force-induced unfolding and refolding.
  • Studied three structurally distinct proteins across a range of constant forces.

Main Results:

  • Observed distinct changes in protein end-to-end fluctuations correlating with unfolding and refolding transitions.
  • Demonstrated that changes in protein compliance during force-induced transitions scale with contour length.
  • Findings align with the sequence-independent freely jointed chain model.

Conclusions:

  • Variance analysis with magnetic tweezers provides high-resolution insights into protein conformational dynamics under mechanical force.
  • The observed scaling of compliance changes supports a polymer physics-based understanding of protein mechanics.
  • This work is vital for understanding mechanosensing and mechanotransduction processes.