Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

You might also read

Related Articles

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

Sort by

Same author

Late-Stage Functionalization of Peptides on the Solid Phase.

Angewandte Chemie (International ed. in English)·2026

Same author

Structure-function analysis of the bacterial ClpE-ClpP AAA+ protease.

The Journal of biological chemistry·2026

Same author

The <i>Schizosaccharomyces pombe</i> Glycosyltransferase Gmh5 is a Functional Homologue of the α-1,6-Mannosyltransferase Mnn10 Crucial for N-Glycan Processing.

Food technology and biotechnology·2026

Same author

NatA engages in multi-factor complexes at the ribosomal polypeptide tunnel exit.

Nature communications·2026

Same author

Pseudouridine increases ribosome stability in a thermophilic eukaryote.

Nucleic acids research·2025

Same author

Structural characterisation of the fungal Pmt4 homodimer.

Nature communications·2025

Same journal

From Fundamental Photophysics to Photocatalysis: Energy Gap Law Analysis of Anion Radical Excited States.

ACS central science·2026

Same journal

Mechanical Taming of Hardy-Cope Rearrangements.

ACS central science·2026

Same journal

Validation of <i>De Novo</i> Designs of Solid-Binding Peptides.

ACS central science·2026

Same journal

These Graphene Experts Are Trying to Close the Reproducibility Gap in Two-Dimensional Materials Research.

ACS central science·2026

Same journal

How to Make a Creamy, Tasty Vegan Camembert.

ACS central science·2026

Same journal

Versatile Pyridinium Trifluoroborate Platform for Facile Preparation of <sup>18</sup>F‑Labeled PET Tracers in Water.

ACS central science·2026

See all related articles

Search research articles

Related Experiment Video

Updated: May 30, 2025

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Strand-Swapped SH3 Domain Dimer with Superoxide Dismutase Activity.

Florian R Häge¹, Merlin Schwan², Marcos Rafael Conde González^1,3

¹Institute of Organic Chemistry, Heidelberg University, Im Neuenheimer Feld 270, 69120 Heidelberg, Germany.

ACS Central Science

|January 27, 2025

Summary

This summary is machine-generated.

Researchers designed a miniaturized superoxide dismutase (SOD) model, SO1, by incorporating a copper-binding site into a small protein. This novel metalloprotein exhibits significant SOD activity, offering a new template for designing binuclear metalloproteins.

More Related Videos

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Related Experiment Videos

Last Updated: May 30, 2025

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Area of Science:

Biochemistry
Biophysical Chemistry
Protein Engineering

Background:

Metalloproteins are crucial for understanding metal-protein interactions and biological functions.
Designing simplified metalloprotein models aids in studying complex biological systems.

Purpose of the Study:

To create a miniaturized superoxide dismutase (SOD) model by incorporating a copper-binding site into a small protein domain (c-Crk-SH3).
To characterize the structure and function of the designed metalloprotein, SO1-Cu.
To evaluate its potential as a template for future metalloprotein designs.

Main Methods:

Protein engineering to create the SO1 miniprotein with a Cu2+-binding site.
Structural characterization using circular dichroism, UV spectroscopy, EPR spectroscopy, and X-ray crystallography.
Functional assessment of superoxide dismutase (SOD) activity.

Main Results:

The SO1 miniprotein formed a strand-swapped dimer with coupled binuclear Type 2-like copper centers.
SO1-Cu demonstrated significant SOD activity, only one order of magnitude lower than natural SOD enzymes.
Its activity was 1-2 orders of magnitude higher than other small SOD models.

Conclusions:

The designed SO1 miniprotein serves as an effective miniaturized SOD model.
The study provides a novel structural template for designing future binuclear metalloproteins with diverse metal ions and functions.
This work highlights the potential of protein engineering in creating functional biomimetic systems.