Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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.

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...

Protein Folding

Protein Folding

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Biophysical characterization of the recombinant merozoite surface protein-3 of Plasmodium vivax.

Biochimica et biophysica acta·2008

Same author

Purification and in vitro characterization of the maltose-binding protein of the plant pathogen Xanthomonas citri.

Protein expression and purification·2005

See all related articles

Search research articles

Related Experiment Video

Updated: May 31, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

¹⁵N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

A spectroscopic-based laboratory experiment for protein conformational studies*.

Carlos Henrique I Ramos¹

¹Centro de Biologia Molecular Estrutural, Laboratório Nacional de Luz Síncrotron, CP 6192, Campinas SP, 13084-971 Brazil, and Departamento de Bioquímica, Instituto de Biologia, Universidade Estadual de Campinas, Campinas SP, Brazil. cramos@lnls.br.

Biochemistry and Molecular Biology Education : a Bimonthly Publication of the International Union of Biochemistry and Molecular Biology

|June 28, 2011

Summary

This experiment teaches basic spectroscopy for studying protein conformational changes. Students learn absorbance, fluorescence, and circular dichroism methods for molecular and structural biology.

More Related Videos

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

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

Related Experiment Videos

Last Updated: May 31, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

¹⁵N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

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

Area of Science:

Molecular Biology
Biochemistry
Structural Biology

Background:

Protein structure and function are central to molecular and structural biology.
Understanding protein conformational changes is crucial for comprehending biological processes and disease mechanisms.
Spectroscopic techniques offer powerful tools for investigating these dynamic changes.

Purpose of the Study:

To describe a practical laboratory experiment for teaching fundamental spectroscopic techniques.
To introduce students to the concept of protein conformational change.
To provide hands-on experience with methods relevant to biochemistry and structural biology.

Main Methods:

Utilizing absorbance spectroscopy for accurate protein concentration determination.
Employing fluorescence spectroscopy to detect alterations in protein microenvironment.
Applying circular dichroism spectroscopy to analyze changes in protein secondary and tertiary structures.

Main Results:

Students gain practical skills in applying spectroscopic methods to biological macromolecules.
The experiment effectively demonstrates how spectroscopic signals correlate with protein conformational states.
The integrated use of absorbance, fluorescence, and circular dichroism provides a comprehensive view of protein structure-function relationships.

Conclusions:

This experiment serves as an effective pedagogical tool for introducing protein conformational changes using basic spectroscopy.
It equips students with essential techniques for future research in molecular biology, biochemistry, and structural biology.
The practical approach enhances understanding of spectroscopic principles and their application in studying protein dynamics.