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

10.5K
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...
10.5K
Protein Folding01:22

Protein Folding

125.3K
Overview
125.3K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

19.3K
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...
19.3K

You might also read

Related Articles

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

Sort by
Same author

Phase Homogeneity and Photothermal Stability in Fully Vacuum-Processed Perovskite Solar Cells.

ACS energy letters·2026
Same author

The MOlecular-Scale Biophysics Research Infrastructure (MOSBRI) Project and its Outcomes.

European biophysics journal : EBJ·2026
Same author

Neuroprotective Effects of Cerium Oxide Nanoparticles During Spaceflight.

Small science·2026
Same author

Metal Halide Perovskite/Chalcohalide Heterojunctions for the Photoinduced Oxidative Coupling of <i>p</i>‑Substituted Thiophenols.

ACS applied nano materials·2026
Same author

Spontaneous Intercalation of Graphene on Sapphire.

Small methods·2026
Same author

DMSO-Free Processing of Tin-Lead Perovskite Thin Films for Solar Cells with Enhanced Stability.

ACS energy letters·2026

Related Experiment Video

Updated: Dec 9, 2025

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
09:33

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

1.3K

Nanopatterning by protein unfolding.

Tiziana Svaldo-Lanero1, Amanda Penco1, Mirko Prato1

  • 1Physics Department, University of Genoa, Via Dodecanneso 33, I-16146 Genova, Italy. cavalleri@fisica.unige.it.

Soft Matter
|September 10, 2020
PubMed
Summary

Common proteins form ordered molecular layers on graphite surfaces. Proteins unfold and reassemble into bilayers, a general behavior observed across different protein types.

More Related Videos

Light-Induced Molecular Adsorption of Proteins Using the PRIMO System for Micro-Patterning to Study Cell Responses to Extracellular Matrix Proteins
09:49

Light-Induced Molecular Adsorption of Proteins Using the PRIMO System for Micro-Patterning to Study Cell Responses to Extracellular Matrix Proteins

Published on: October 11, 2019

12.9K
DNA Origami-Mediated Substrate Nanopatterning of Inorganic Structures for Sensing Applications
08:59

DNA Origami-Mediated Substrate Nanopatterning of Inorganic Structures for Sensing Applications

Published on: September 27, 2019

12.0K

Related Experiment Videos

Last Updated: Dec 9, 2025

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
09:33

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

1.3K
Light-Induced Molecular Adsorption of Proteins Using the PRIMO System for Micro-Patterning to Study Cell Responses to Extracellular Matrix Proteins
09:49

Light-Induced Molecular Adsorption of Proteins Using the PRIMO System for Micro-Patterning to Study Cell Responses to Extracellular Matrix Proteins

Published on: October 11, 2019

12.9K
DNA Origami-Mediated Substrate Nanopatterning of Inorganic Structures for Sensing Applications
08:59

DNA Origami-Mediated Substrate Nanopatterning of Inorganic Structures for Sensing Applications

Published on: September 27, 2019

12.0K

Area of Science:

  • Materials Science
  • Biophysics
  • Surface Chemistry

Background:

  • Ordered molecular layers are crucial for advanced materials.
  • Protein adsorption on surfaces is a key phenomenon in biotechnology and nanotechnology.
  • Controlling protein assembly at the nanoscale is challenging.

Purpose of the Study:

  • To investigate the self-assembly behavior of proteins on highly oriented pyrolytic graphite (HOPG).
  • To determine if protein adsorption on HOPG leads to ordered nanoscale structures.
  • To assess the generality of this protein self-assembly behavior.

Main Methods:

  • Adsorption of common proteins onto the hydrophobic surface of HOPG.
  • Characterization of the resulting molecular layers using nanoscale patterning techniques.
  • Analysis of protein structural changes and re-assembly on the surface.

Main Results:

  • Proteins adsorbed onto HOPG form nanoscale molecular layers with long-range order.
  • Proteins undergo denaturation, losing native folding upon adsorption.
  • Polypeptide chains re-assemble into a stable molecular bilayer structure.
  • This self-assembly behavior is consistent across various proteins, regardless of their specific structures.

Conclusions:

  • Highly oriented pyrolytic graphite (HOPG) provides a suitable surface for creating ordered protein-based molecular layers.
  • Protein adsorption on HOPG results in a generalizable self-assembly mechanism forming molecular bilayers.
  • This finding has implications for designing novel nanomaterials and understanding protein-surface interactions.