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

Understanding Mass Spectrometry: From Ion Generation to Spectral Interpretation.

Journal of mass spectrometry : JMS·2026
Same author

Mapping Functionally Relevant Tractable Lysines of Challenging Protein Targets by Covalent Fragment Screening.

Chembiochem : a European journal of chemical biology·2026
Same author

Mapping the Substrate Specificity Landscape of PAD2 and PAD4 Enzymes.

Chembiochem : a European journal of chemical biology·2026
Same author

Harmonized <sup>1</sup>H NMR Workflow Enables Quantitative Betaine Determination from Nontargeted Metabolite Profiling Using Internal and External Standards<sup>‡‡‡‡‡</sup>.

Analytical chemistry·2026
Same author

Deterministic Acceptance Limits for Statistical Equivalence Testing in Hydrogen/Deuterium Exchange Mass Spectrometry.

Journal of the American Society for Mass Spectrometry·2026
Same author

Avoiding Mitochondrial Apoptosis by the Bcl-2-Driven Bax Oligomerization on Membrane Surfaces.

ACS chemical biology·2026

Related Experiment Video

Updated: Sep 17, 2025

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
07:11

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

2.8K

Photochemical and Structural Studies on Cyclic Peptide Models.

Tamás Milán Nagy1, Krisztina Knapp2, Eszter Illyés3

  • 1Department of Inorganic and Analytical Chemistry, University of Debrecen, H-4032 Debrecen, Egyetem tér 1, Hungary. tamasmilan.nagy@science.unideb.hu.

Molecules (Basel, Switzerland)
|September 12, 2018
PubMed
Summary

UV light damages proteins by breaking disulfide bonds, a process linked to tryptophan. This study used peptide models to show how tryptophan

Keywords:
MDNMRUV irradiationcyclopeptidesdisulfide bridgesphotolysis

More Related Videos

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

10.9K
Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Published on: January 27, 2016

12.0K

Related Experiment Videos

Last Updated: Sep 17, 2025

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
07:11

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

2.8K
Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

10.9K
Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Published on: January 27, 2016

12.0K

Area of Science:

  • Biochemistry
  • Photochemistry
  • Molecular Biology

Background:

  • Ultra-violet (UV) irradiation significantly affects protein structure and function.
  • This damage is hypothesized to involve tryptophan-mediated photolysis of disulfide bonds.

Purpose of the Study:

  • To investigate the correlation between photoexcitation of tryptophan (Trp) residues and disulfide bond reduction in polypeptides.
  • To analyze tryptophan-containing cyclic peptide models to understand UV-induced photolysis.

Main Methods:

  • Molecular mechanics (MM) and molecular dynamics (MD) simulations to determine distances between Trp and disulfide bonds.
  • Synthesis and analysis of cyclic peptides using nuclear magnetic resonance (NMR) spectroscopy.
  • Photolytic degradation studies monitored by fluorescence spectroscopy and mass spectrometry (MS).

Main Results:

  • MM calculations indicated a ~5 Å distance between Trp side chains and disulfide bridges in models.
  • NMR and MD simulations confirmed MM findings.
  • Photolysis experiments revealed disulfide bond cleavage and formation of various photooxidation products.

Conclusions:

  • Structural proximity between Trp residues and disulfide bonds facilitates UV-induced photolysis.
  • Secondary photolytic processes contribute to the complexity of UV-induced protein damage.
  • These findings provide insights into the photochemistry of proteins and peptides.