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
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

6.3K
Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
6.3K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

7.1K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
7.1K
The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

4.6K
ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
4.6K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

28.3K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
28.3K

You might also read

Related Articles

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

Sort by
Same author

<i>In Vivo</i> Activity of Antimicrobial Peptoid Oligomers against HSV-1 in a Mouse Model of Herpes Labialis.

ACS infectious diseases·2026
Same author

Quantitative holographic agglutination assay for immunoglobulin A.

Biomedical optics express·2026
Same author

Structural and Positional Effects of Peptoid Residues on Triple Helix Stability.

Biomacromolecules·2026
Same author

Miniprotein inhibitors of the <i>Staphylococcus aureus</i> efflux transporter NorA.

bioRxiv : the preprint server for biology·2026
Same author

Native Chemical Ligation of Peptoid Oligomers.

Biochemistry·2026
Same author

Conformation-aware structure prediction of antigen-recognizing immune proteins.

mAbs·2025

Related Experiment Video

Updated: Mar 26, 2026

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

9.4K

A Miniature Protein Stabilized by a Cation-π Interaction Network.

Timothy W Craven1,2, Min-Kyu Cho1, Nathaniel J Traaseth1

  • 1Department of Chemistry, New York University , 100 Washington Square East, New York, New York 10003, United States.

Journal of the American Chemical Society
|January 27, 2016
PubMed
Summary

Researchers engineered a miniature protein using cation-π interactions, mimicking natural "WSXWS motifs." This design stabilizes a unique fold, demonstrating a novel strategy for protein stabilization and design.

More Related Videos

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells
08:38

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

Published on: March 3, 2015

14.0K
Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
08:15

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

4.8K

Related Experiment Videos

Last Updated: Mar 26, 2026

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

9.4K
Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells
08:38

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

Published on: March 3, 2015

14.0K
Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
08:15

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

4.8K

Area of Science:

  • Protein engineering and structural biology.
  • Computational and biophysical chemistry.

Background:

  • Protein folding relies on noncovalent interactions for stable tertiary structures.
  • Cation-π interactions, particularly in "WSXWS motifs," are crucial for stabilizing protein cores.

Purpose of the Study:

  • To emulate cation-π interaction networks for stabilizing miniature protein cores.
  • To design and validate a 19-residue miniature protein with a specific topology.

Main Methods:

  • Designed a miniature protein sequence featuring interdigitated arginine and tryptophan residues.
  • Determined the protein's tertiary structure using Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Validated the fold through mutagenesis of the cation-π network and comparison with disulfide-bridged structures.

Main Results:

  • Successfully recapitulated a stable β-strand:loop:PPII-helix topology in the miniature protein.
  • Demonstrated that the engineered cation-π network is essential for stabilizing the compact fold.
  • NMR data confirmed the structure and the role of specific residues in stabilization.

Conclusions:

  • A network of cation-π interactions can effectively stabilize the core of miniature proteins.
  • This study provides a blueprint for designing thermostable protein structures using emulated natural motifs.
  • The findings highlight the importance of coordinated noncovalent interactions in protein folding and stability.