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

IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration01:16

IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration

1.7K
A covalently bonded heteronuclear diatomic molecule can be modeled as two vibrating masses connected by a spring. The vibrational frequency of the bond can be expressed using an equation derived from Hooke's law, which describes how the force applied to stretch or compress a spring is proportional to the displacement of the spring. In this case, the atoms behave like masses, and the bond acts like a spring.
According to Hooke's law, the vibrational frequency is directly proportional to...
1.7K
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

926
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...
926
¹H NMR: Long-Range Coupling01:27

¹H NMR: Long-Range Coupling

2.0K
The coupling interactions of nuclei across four or more bonds are usually weak, with J values less than 1 Hz. While these are usually not observed in spectra, the presence of multiple bonds along the coupling pathway can result in observable long-range coupling.
In alkenes, spin information is communicated via σ–π overlap, as seen in allylic (four-bond) and homoallylic (five-bond) couplings. These coupling interactions are stronger when the σ bond is parallel to the alkene...
2.0K
Spin–Spin Coupling Constant: Overview01:08

Spin–Spin Coupling Constant: Overview

1.0K
In bromoethane, the three methyl protons are coupled to the two methylene protons that are three bonds away. In accordance with the n+1 rule, the signal from the methyl protons is split into three peaks with 1:2:1 relative intensities. The methylene protons appear as a quartet, with the relative intensities of 1:3:3:1.
Qualitatively, any spin plus-half nucleus polarizes the spins of its electrons to the minus-half state. Consequently, the paired electron in the hydrogen–carbon bond must...
1.0K
IR Spectrum Peak Splitting: Symmetric vs Asymmetric Vibrations01:08

IR Spectrum Peak Splitting: Symmetric vs Asymmetric Vibrations

1.2K
Identical bonds within a polyatomic group can stretch symmetrically (in-phase) or asymmetrically (out-of-phase). Similar to hydrogen bonding, these vibrations also influence the shape of the IR peak. Generally, asymmetric stretching frequencies are higher than symmetric stretching frequencies. For example, primary amines exhibit two distinct IR peaks between 3300–3500 cm−1 corresponding to the symmetric and asymmetric N-H stretching, while secondary amines exhibit a single...
1.2K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.1K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
3.1K

You might also read

Related Articles

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

Sort by
Same author

Self-heating-induced blocking in nanopores enables neuromorphic ionic computing.

Nature communications·2026
Same author

Longitudinal Trajectories and Determinants of Fear of Falling in Post-Stroke Patients.

Journal of nursing scholarship : an official publication of Sigma Theta Tau International Honor Society of Nursing·2026
Same author

Hypoxia-Inducible Factor Prolyl Hydroxylase EGLN3 Stabilizes Atherosclerotic Plaques in ApoE<sup>-/-</sup> Mice Independently of Its Catalytic Activity.

Arteriosclerosis, thrombosis, and vascular biology·2026
Same author

Pressure Driven Non-monotonic Gating in Tunable Polydimethylsiloxane Nanopores Regulates DNA Translocation.

ACS nano·2026
Same author

A proliferation-inducing ligand enhances the anti-tumor effect of BCMA CAR T-cell through inhibition of soluble BCMA.

Biochimica et biophysica acta. Molecular basis of disease·2026
Same author

DiRT v2.0: An Optimized Pipeline for Detecting Dicistronic tRNA-mRNA Transcripts in Plants.

Bio-protocol·2026

Related Experiment Video

Updated: Sep 20, 2025

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

2.2K

Length-Dependent Collective Vibrational Dynamics in Alpha-Helices.

Zhenyu Zhang1, Mu Chen1, Lijian Zhan1

  • 1Jiangsu Key Laboratory for Design and Manufacture of Micro-Nano Biomedical Instruments, School of Mechanical Engineering, Southeast University, Nanjing, 211189, China.

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry
|June 9, 2022
PubMed
Summary

Researchers studied protein vibrations to link structure and function, aiding in new protein design. Understanding alpha-helix dynamics is key for creating novel proteins.

More Related Videos

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

1.9K
Preparation of Extracellular Matrix Protein Fibers for Brillouin Spectroscopy
07:19

Preparation of Extracellular Matrix Protein Fibers for Brillouin Spectroscopy

Published on: September 15, 2016

10.5K

Related Experiment Videos

Last Updated: Sep 20, 2025

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

2.2K
High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

1.9K
Preparation of Extracellular Matrix Protein Fibers for Brillouin Spectroscopy
07:19

Preparation of Extracellular Matrix Protein Fibers for Brillouin Spectroscopy

Published on: September 15, 2016

10.5K

Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Chemistry

Background:

  • Proteins are essential biomolecules with complex structures that dictate their functions.
  • Understanding the dynamic behavior of proteins, such as vibrational motions, is crucial for deciphering their mechanisms of action.
  • Alpha-helices are common secondary structures in proteins, and their collective motions are fundamental to protein dynamics.

Purpose of the Study:

  • To investigate the collective vibrational motions of alpha-helices within proteins.
  • To establish a connection between protein structure, dynamics, and function.
  • To provide insights for the field of de novo protein design.

Main Methods:

  • Analysis of collective vibrational motions within protein structures.
  • Computational modeling and simulation techniques to study alpha-helix dynamics.
  • Correlation of vibrational patterns with known protein functions.

Main Results:

  • Identified specific collective vibrational modes in alpha-helices.
  • Demonstrated a clear link between these vibrational motions and protein structural stability.
  • Showcased how understanding these dynamics can inform protein engineering.

Conclusions:

  • Collective vibrational motions of alpha-helices are integral to protein structure-function relationships.
  • This research offers a novel approach for predicting and designing protein functions.
  • The findings support the development of advanced de novo protein design strategies.