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Related Concept Videos

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

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

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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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Related Experiment Video

Updated: Jun 6, 2026

Synthesis of Cyclic Polymers and Characterization of Their Diffusive Motion in the Melt State at the Single Molecule Level
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Synthesis of Cyclic Polymers and Characterization of Their Diffusive Motion in the Melt State at the Single Molecule Level

Published on: September 26, 2016

Temperature-cycle single-molecule FRET microscopy on polyprolines.

Haifeng Yuan1, Ted Xia, Benjamin Schuler

  • 1Molecular Nano-Optics and Spins, Leiden Institute of Physics, Leiden University, Leiden, The Netherlands.

Physical Chemistry Chemical Physics : PCCP
|December 15, 2010
PubMed
Summary
This summary is machine-generated.

Single-molecule temperature-cycle microscopy enables observing microsecond dynamics by tracking FRET changes in labeled polyprolines. This technique reveals rapid conformational changes previously inaccessible, advancing single-molecule biophysics.

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Last Updated: Jun 6, 2026

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Studying DNA Looping by Single-Molecule FRET

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Area of Science:

  • Biophysics
  • Single-molecule spectroscopy
  • Polymer dynamics

Background:

  • Traditional methods limit real-time single-molecule dynamics to millisecond timescales.
  • Molecular fluorescence rates typically restrict time resolution.
  • Studying rapid conformational changes at the microsecond level is challenging.

Purpose of the Study:

  • To develop and apply single-molecule temperature-cycle microscopy for probing microsecond dynamics.
  • To investigate the conformational dynamics of single FRET-labeled polyprolines.
  • To achieve time resolution at the microsecond scale for single-molecule studies.

Main Methods:

  • Single-molecule fluorescence resonance energy transfer (FRET) microscopy.
  • Temperature-cycling of FRET-labeled polyprolines in glycerol.
  • Real-time monitoring of donor and acceptor fluorescence signals.

Main Results:

  • Observed FRET efficiency distributions deviating from isotropic models, suggesting label orientation influence.
  • Detected significant FRET changes within microseconds at 250 K, attributed to label reorientation.
  • Tracked FRET efficiency over 2000 cycles, showing switching between two conformations.

Conclusions:

  • Single-molecule temperature-cycle microscopy successfully probes microsecond dynamics.
  • Oligopeptide conformational changes occur rapidly, influenced by fluorescent label orientation.
  • This technique offers new possibilities for studying ultrafast biomolecular dynamics at the single-molecule level.