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-protein Interfaces02:04

Protein-protein Interfaces

15.0K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
15.0K
Protein Networks02:26

Protein Networks

4.7K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.7K
DNA Helicases00:55

DNA Helicases

24.8K
DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
24.8K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

20.7K
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...
20.7K
Mechanical Protein Functions01:58

Mechanical Protein Functions

5.8K
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
5.8K

You might also read

Related Articles

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

Sort by
Same author

Copy-back RNA synthesis by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir.

Science advances·2026
Same author

16S rRNA Gene-Based Metagenomic Analysis of Rhizosphere Soil Bacteria in Arkansas Rice Crop Fields.

Agronomy (Basel, Switzerland)·2026
Same author

RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA.

Cell reports·2026
Same author

Structural heterogeneity and functional convergence of transposable elements.

Frontiers in genetics·2026
Same author

ZNF16 is a nucleolar-associated protein that regulates expression of rDNA and cancer-associated genes.

Biology open·2025
Same author

Response to the commentary by Melidis et al. on "Untargeted CUT&Tag reads are enriched at accessible chromatin and restrict identification of potential G4-forming sequences in G4-targeted CUT&Tag experiments".

Nucleic acids research·2025

Related Experiment Video

Updated: Mar 22, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays
07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

18.7K

Protein-protein interaction analysis for functional characterization of helicases.

Boris L Zybailov1, Alicia K Byrd1, Galina V Glazko2

  • 1Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, United States.

Methods (San Diego, Calif.)
|April 20, 2016
PubMed
Summary

Understanding protein interactions is key to the function of helicases, enzymes crucial for DNA replication, transcription, and repair. This review focuses on proteomics methods like affinity pull-downs and cross-linking mass spectrometry for analyzing these essential helicase interactions.

Keywords:
Biological networksChemical cross-linkingHelicaseMass spectrometryProtein oligomerizationProtein-protein interactions

More Related Videos

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

19.1K
Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

8.6K

Related Experiment Videos

Last Updated: Mar 22, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays
07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

18.7K
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

19.1K
Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

8.6K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Proteomics

Background:

  • Helicases are vital enzymes in nucleic acid metabolism, essential for DNA replication, transcription, and repair.
  • Understanding their oligomerization state and protein interactions is crucial for elucidating helicase function.

Purpose of the Study:

  • To review current proteomics methods for analyzing protein-protein interactions.
  • To discuss the application of these methods in studying specific helicases, Pif1 and DDX3.
  • To provide guidelines for implementing these techniques in helicase functional analysis.

Main Methods:

  • Focus on affinity pull-down assays.
  • Focus on chemical cross-linking followed by mass spectrometry.
  • Review of advantages and limitations of these proteomics techniques.

Main Results:

  • Proteomics methods, particularly affinity pull-downs and cross-linking mass spectrometry, are powerful tools for studying helicase interactions.
  • These methods allow for the definition of helicase oligomerization states and transient/persistent protein interactions.
  • Case studies of Pif1 and DDX3 demonstrate the practical application of these techniques.

Conclusions:

  • Affinity pull-downs and cross-linking mass spectrometry are key techniques for functional analysis of helicases.
  • These methods provide essential insights into the dynamic protein interaction networks of helicases.
  • Guidelines are provided for effective implementation in helicase research.