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

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.

Conformity

Conformity

Conformity is the change in a person’s behavior to go along with the group, even if that person does not agree with the group.

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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...

Conformations of Butane

Conformations of Butane

Unlike ethane and propane that have only two major conformations, butane has more than two conformers. The staggered form of butane in which the bulky methyl groups on the two carbons are placed on opposite sides, that is, at a dihedral angle of 180°, is the lowest energy, most stable form — called the anti conformer. This conformation is stabilized due to the absence of steric repulsion between the largely spaced out methyl groups. The other two staggered conformations are...

Conformations of Cycloalkanes

Conformations of Cycloalkanes

Adolf von Baeyer attempted to explain the instabilities of small and large cycloalkane rings using the concept of angle strain — the strain caused by the deviation of bond angles from the ideal 109.5° tetrahedral value for sp3 hybridized carbons. However, while cyclopropane and cyclobutane are strained, as expected from their highly compressed bond angles, cyclopentane is more strained than predicted, and cyclohexane is virtually strain-free. Hence, Baeyer’s theory that...

Conformations of Cyclohexane

Conformations of Cyclohexane

Cyclohexane does not exist in a planar form due to the high angle and torsional strain it would experience in the planar structure. Instead, it adopts non-planar chair and boat conformations.
The chair form is the most stable and derives its name from its resemblance to the “easy chair.” In the chair conformation, two carbon atoms are arranged out-of-plane — one above and one below, minimizing the torsional strain. In the chair form, the bond angle is very close to the ideal...

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Related Experiment Video

Updated: Jan 31, 2026

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

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

Published on: June 29, 2021

Exploring Protein Conformational Landscapes Using High-Pressure NMR.

Julien Roche¹, Catherine A Royer², Christian Roumestand³

¹Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, United States.

Methods in Enzymology

|January 7, 2019

Summary

Mapping protein conformational landscapes using high pressure and Nuclear Magnetic Resonance (NMR) spectroscopy reveals crucial insights into protein function and homeostasis. This powerful combination aids in understanding and modulating protein structure.

Keywords:

High pressure Intermediates NMR Protein folding Transition state

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Last Updated: Jan 31, 2026

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

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Area of Science:

Biochemistry
Structural Biology
Biophysics

Background:

Protein conformational landscapes dictate function and proteostasis.
Understanding these landscapes is key to modulating protein conformation.
Detailed mapping is essential for biological insights.

Purpose of the Study:

To detail protein conformational landscapes.
To explore the utility of high pressure and NMR spectroscopy in characterizing protein conformational transitions.
To understand the role of pressure in protein structure perturbation.

Main Methods:

Utilizing high pressure combined with Nuclear Magnetic Resonance (NMR) spectroscopy.
Leveraging pressure as a subtle perturbation to favor intermediate states.
Employing NMR's residue-specific observables to probe local structural properties.

Main Results:

High pressure NMR effectively characterizes protein conformational transitions.
Pressure perturbs protein structure by eliminating solvent-excluded void volume.
NMR provides multifaceted, residue-specific data on protein states.

Conclusions:

High pressure and NMR spectroscopy offer a powerful approach for mapping protein conformational landscapes.
This technique aids in characterizing intermediate and excited protein states.
Understanding these landscapes is crucial for protein function and proteostasis.