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

You might also read

Related Articles

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

Sort by
Same author

Small Molecule Activators of Protein Phosphatase 2A Exert Global Stabilizing Effects on the Scaffold PR65.

JACS Au·2026
Same author

Calmodulin assists during co-translational folding of the K<sub>V</sub>7.2 channel calcium responsive domain.

Protein science : a publication of the Protein Society·2026
Same author

Cotranslational Assembly of Oligomeric Proteins.

Annual review of biochemistry·2026
Same author

NAC promotes co-translational protein folding at the ribosomal tunnel exit.

Molecular cell·2026
Same author

Human gut M cells resemble dendritic cells and present gluten antigen.

Nature·2025
Same author

Cell tracking with accurate error prediction.

Nature methods·2025
Same journal

Nanotechnology-Stem Cell Strategies in 3D Glioblastoma Organoid: Targeting Glioma Stem Cells Within a Complex Tumor Microenvironment.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Mapping the 3D Chromosome Organization of a Biosynthetic Gene Cluster by Capture Hi-C (CHi-C).

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Mapping the 3D Chromosome Organization of Streptomyces by Hi-C.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

CUT&Tag Epigenomic Profiling of Biosynthetic Gene Clusters in Arabidopsis thaliana.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Rhizobium rhizogenes-Mediated Hairy Root Transformation Protocol for Lotus japonicus and Other Legumes.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Characterization of Bioactive Saponins from Sea Cucumbers.

Methods in molecular biology (Clifton, N.J.)·2026
See all related articles

Related Experiment Video

Updated: Jul 13, 2025

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

11.1K

Protein Tethering for Single-Molecule Force Spectroscopy.

Mario J Avellaneda1, Eline J Koers1, Vanda Sunderlikova1

  • 1AMOLF, Amsterdam, The Netherlands.

Methods in Molecular Biology (Clifton, N.J.)
|October 12, 2023
PubMed
Summary
This summary is machine-generated.

This study presents a universal method for attaching DNA tethers to proteins, crucial for optical tweezers experiments. This technique enables efficient study of protein folding and interactions.

Keywords:
Cysteine-independent linkagesProtein foldingProtein-DNA chimeraSingle-molecule detection

More Related Videos

Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers
10:08

Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers

Published on: July 25, 2012

11.6K
Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
06:45

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

Published on: February 28, 2019

8.8K

Related Experiment Videos

Last Updated: Jul 13, 2025

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

11.1K
Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers
10:08

Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers

Published on: July 25, 2012

11.6K
Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
06:45

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

Published on: February 28, 2019

8.8K

Area of Science:

  • Biophysics
  • Molecular Biology
  • Biochemistry

Background:

  • Optical tweezers are vital for studying protein folding dynamics and interactions.
  • Efficiently attaching DNA handles to proteins is a significant challenge in single-molecule biophysics.
  • Understanding protein conformational states requires robust molecular manipulation techniques.

Purpose of the Study:

  • To develop a universal and efficient method for covalently linking DNA tethers to proteins.
  • To enable the study of protein interactions and folding using optical tweezers.
  • To overcome limitations in current DNA-protein attachment strategies.

Main Methods:

  • A novel covalent linking strategy for DNA tethers up to 5000 base pairs.
  • Applicable to proteins with or without native cysteines.
  • Detailed protocol for reproducible DNA-protein conjugation.

Main Results:

  • Successful covalent attachment of long DNA tethers to diverse proteins.
  • Demonstrated versatility of the method for proteins with and without native cysteines.
  • Established an efficient and stable DNA handle attachment for optical tweezers.

Conclusions:

  • The developed method provides a universal solution for DNA tethering in protein studies.
  • Facilitates advanced single-molecule investigations of protein behavior.
  • Enhances the capabilities of optical tweezers in molecular biophysics research.