Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Molecular Geometry and Dipole Moments02:36

Molecular Geometry and Dipole Moments

14.0K
The VSEPR theory can be used to determine the electron pair geometries and molecular structures as follows:
14.0K
Electric Dipoles and Dipole Moment01:30

Electric Dipoles and Dipole Moment

5.5K
Consider two charges of equal magnitude but opposite signs. If they cannot be separated by an external electric field, the system is called a permanent dipole. For example, the water molecule is a dipole, making it a good solvent.
Theoretically, studying electric dipoles leads to understanding why the resultant electric forces around us are weak. Since electric forces are strong, remnant net charges are rare. Hence, the interaction between dipoles helps us understand electrical interactions in...
5.5K
Protein Folding01:22

Protein Folding

121.3K
Overview
121.3K
Induced Electric Dipoles01:28

Induced Electric Dipoles

4.4K
A permanent electric dipole orients itself along an external electric field. This rotation can be quantified by defining the potential energy because the external torque does work in rotating it. Then, the potential energy is minimum at the parallel configuration and maximum at the antiparallel configuration. While the former is a stable equilibrium, the latter is an unstable equilibrium.
Since the absolute value of potential energy holds no physical meaning, its zero value can be chosen as per...
4.4K
Molecular Shape and Polarity03:37

Molecular Shape and Polarity

62.0K
Dipole Moment of a Molecule
62.0K
IR Spectrum Peak Intensity: Dipole Moment01:20

IR Spectrum Peak Intensity: Dipole Moment

817
The dipole moment of a bond is the product of the partial charge on either atom and the distance between them. Dipole moments influence the efficiency of IR absorption and the peak intensity. When a bond with a dipole moment is placed in an electric field, the direction of the field determines if the bond is compressed or stretched. Electromagnetic radiation consists of an electric field component that rapidly reverses direction. It follows that polar bonds are alternately stretched and...
817

You might also read

Related Articles

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

Sort by
Same author

Advances in Probing Amyloid Heterogeneity Using Vibrational Spectroscopy and Imaging.

The journal of physical chemistry. B·2025
Same author

Refining Structural Analysis of Proteins: Automated Methods to Measure Transition Dipole Strength of Single Residues.

The journal of physical chemistry. B·2025
Same author

Deciphering the Molecular Dance: Exploring the Dynamic Interplay Between Mouse Insulin B9-23 Peptides and their Variants.

Biochemistry·2024
Same author

Suppressing sidechain modes and improving structural resolution for 2D IR spectroscopy via vibrational lifetimes.

The Journal of chemical physics·2024
Same author

Copper-Phosphido Catalysis: Enantioselective Addition of Phosphines to Cyclopropenes.

Angewandte Chemie (International ed. in English)·2023
Same author

Determining the impact of gold nanoparticles on amyloid aggregation with 2D IR spectroscopy.

The Journal of chemical physics·2023

Related Experiment Video

Updated: Sep 12, 2025

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

15.6K

Transition Dipole Strength as a Quantitative Tool for Protein Secondary Structure Analysis.

Amanda L Cao1, Lindsey M Weissman1, Lauren E Buchanan1

  • 1Department of Chemistry, Vanderbilt University, Nashville, Tennessee 37235, United States.

The Journal of Physical Chemistry. B
|August 7, 2025
PubMed
Summary

Transition dipole strength (TDS) analysis, an extension of 2D IR spectroscopy, reveals protein structures. TDS correlates with alpha-helix length, aiding in predicting protein structures and understanding complex folding dynamics.

More Related Videos

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
13:26

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

62.0K
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

68.9K

Related Experiment Videos

Last Updated: Sep 12, 2025

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

15.6K
Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
13:26

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

62.0K
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

68.9K

Area of Science:

  • Protein structure and dynamics
  • Vibrational spectroscopy
  • Biophysical chemistry

Background:

  • Protein folding is complex and difficult to study experimentally.
  • Two-dimensional infrared (2D IR) spectroscopy offers insights into molecular dynamics.
  • Transition dipole strength (TDS) analysis is an emerging technique to probe protein structures.

Purpose of the Study:

  • To investigate the utility of transition dipole strength (TDS) analysis for determining protein structural information.
  • To establish correlations between TDS values and secondary structure lengths in peptides.
  • To explore the application of TDS analysis in complex protein architectures.

Main Methods:

  • Systematic characterization of TDS in model alpha-helical peptides.
  • Analysis of TDS variations in beta-sheet structures with differing higher-order organization.
  • Extrapolation of TDS-based structure determination methods for globular proteins.

Main Results:

  • A linear correlation was found between TDS values and alpha-helical length, enabling prediction of maximum helical lengths in proteins.
  • TDS interpretation for beta-sheet structures is complex due to significant variations based on folding and complex formation.
  • The study demonstrates TDS analysis's potential for elucidating structural dynamics inaccessible by other methods.

Conclusions:

  • TDS analysis is a powerful tool for protein structure elucidation, particularly for complex architectures.
  • Further research is needed to understand the relationship between higher-order structures and vibrational delocalization in TDS.
  • This technique offers new avenues for studying protein folding dynamics and structural heterogeneity.