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

Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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...

You might also read

Related Articles

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

Sort by
Same author

DHHC3-dependent S-Acylation of CRY1 regulates its subcellular localization and repressor function in the circadian clock.

bioRxiv : the preprint server for biology·2026
Same author

OMAMA-DB: the Oregon-Massachusetts Mammography Database.

Journal of medical imaging (Bellingham, Wash.)·2026
Same author

How Functional Variants Reconfigure the Rac2 Conformational Landscape.

bioRxiv : the preprint server for biology·2026
Same author

DNA deformability in sequence-dependent capture of E. coli gyrase.

Nature communications·2026
Same author

Functional and structural basis of a hypermorphic TRPC3 variant.

Science advances·2026
Same author

FOXM1-Specific TCR-Engineered T Cells Target Non-Small Cell Lung Cancer.

Cancer immunology research·2026
Same journal

Characterization of putative proteins encoded by variable ORFs in white spot syndrome virus genome.

BMC structural biology·2019
Same journal

Correction to: Classification of the human THAP protein family identifies an evolutionarily conserved coiled coil region.

BMC structural biology·2019
Same journal

Effect of low complexity regions within the PvMSP3α block II on the tertiary structure of the protein and implications to immune escape mechanisms.

BMC structural biology·2019
Same journal

QRNAS: software tool for refinement of nucleic acid structures.

BMC structural biology·2019
Same journal

Classification of the human THAP protein family identifies an evolutionarily conserved coiled coil region.

BMC structural biology·2019
Same journal

A new technique for predicting intrinsically disordered regions based on average distance map constructed with inter-residue average distance statistics.

BMC structural biology·2019
See all related articles

Related Experiment Video

Updated: Jun 12, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
11:55

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling

Published on: May 29, 2011

Tracing conformational changes in proteins.

Nurit Haspel1, Mark Moll, Matthew L Baker

  • 1Department of Computer Science, Rice University, Houston, TX 77005, USA.

BMC Structural Biology
|May 22, 2010
PubMed
Summary
This summary is machine-generated.

This study introduces a novel robotics-inspired method to efficiently trace large-scale protein conformational changes. The approach uses a coarse-grained model to identify low-energy pathways, aiding in understanding protein function.

More Related Videos

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

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

Published on: June 27, 2014

Related Experiment Videos

Last Updated: Jun 12, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
11:55

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling

Published on: May 29, 2011

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

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

Published on: June 27, 2014

Area of Science:

  • Computational Biology
  • Biophysics
  • Protein Dynamics

Background:

  • Proteins undergo significant conformational changes crucial for their function.
  • Understanding these dynamic changes is key to elucidating protein mechanisms.
  • Traditional methods for conformational search are computationally intensive and limited for large-scale motions.

Purpose of the Study:

  • To investigate a robotics-inspired computational method for tracing large-scale protein conformational changes.
  • To assess the efficiency and applicability of this method for modeling protein dynamics.

Main Methods:

  • Utilized a coarse-grained energy function with backbone and limited side chain representation.
  • Applied a robotics-inspired algorithm to search conformational space.
  • Tested the method on four well-characterized medium to large proteins.

Main Results:

  • Successfully traced low-energy conformational pathways efficiently, even with limited input data.
  • Demonstrated the method's ability to capture large-scale conformational changes.
  • Generated conformational pathways that can be refined for physiological relevance.

Conclusions:

  • The proposed method effectively captures large-scale protein conformational changes.
  • Generated pathways align with experimental data and existing computational findings.
  • This represents a significant advancement for modeling complex biological systems.