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 Experiment Videos

Cation-pi interaction in model alpha-helical peptides.

Zhengshuang Shi1, C Anders Olson, Neville R Kallenbach

  • 1Department of Chemistry, New York University, New York 10003, USA.

Journal of the American Chemical Society
|March 28, 2002
PubMed
Summary
This summary is machine-generated.

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

Heterologous saRNA Prime, DNA Dual-Antigen Boost SARS-CoV-2 Vaccination Elicits Robust Cellular Immunogenicity and Cross-Variant Neutralizing Antibodies.

Frontiers in immunology·2022
Same author

Rapid identification of neutralizing antibodies against SARS-CoV-2 variants by mRNA display.

Cell reports·2022
Same author

Rapid Identification of Neutralizing Antibodies against SARS-CoV-2 Variants by mRNA Display.

bioRxiv : the preprint server for biology·2021
Same author

Intranasal plus subcutaneous prime vaccination with a dual antigen COVID-19 vaccine elicits T-cell and antibody responses in mice.

Scientific reports·2021
Same author

An ACE2 Triple Decoy that neutralizes SARS-CoV-2 shows enhanced affinity for virus variants.

Scientific reports·2021
Same author

Hydration effects on Leu's polyproline II population in AcLXPNH<sub>2</sub>.

Chemical communications (Cambridge, England)·2018
Same journal

Gas-Responsive Metal-Organic Frameworks for Adaptive Thermal Energy Storage with Tunable Charge-Discharge Temperatures.

Journal of the American Chemical Society·2026
Same journal

Engineering a Thiamine-Dependent Benzoylformate Decarboxylase for Stereodivergent Radical C(sp<sup>3</sup>)-C(sp<sup>3</sup>) Bond Formation.

Journal of the American Chemical Society·2026
Same journal

Accelerated Directional Proton-Coupled Electron Transfer Enabled by Intrinsic Dipole Field in Biomimetic α-Helical Structure.

Journal of the American Chemical Society·2026
Same journal

Alternating Current-Driven Hydrogen Isotope Labeling of Aliphatic Amines Using 1,3-Propanedithiol as an Efficient Hydrogen Atom Transfer Reagent.

Journal of the American Chemical Society·2026
Same journal

Two-Dimensional van der Waals Polar Metal MoOBr<sub>2</sub>.

Journal of the American Chemical Society·2026
Same journal

Negatively Curved Chiral Bilayer Nanographene.

Journal of the American Chemical Society·2026
See all related articles

Cation-pi interactions involving tryptophan and arginine significantly enhance peptide helix stability when oriented correctly. This interaction is stronger than phenylalanine-arginine, offering insights into protein stability.

Area of Science:

  • Biochemistry
  • Chemical Physics
  • Molecular Biology

Background:

  • Cation-pi interactions are crucial in biological and chemical systems.
  • Understanding these interactions aids in predicting protein structure and stability.

Purpose of the Study:

  • To investigate the impact of cation-pi interactions on peptide helicity.
  • To quantify the energetic contribution of specific residue pairings (Trp/Arg, Phe/Arg) to helix stability.

Main Methods:

  • Circular Dichroism (CD) spectroscopy to assess peptide helicity.
  • Nuclear Magnetic Resonance (NMR) spectroscopy to analyze molecular interactions.
  • Experimental determination of free energy contributions to helix stability.

Main Results:

Related Experiment Videos

  • A Trp-->Arg (i, i + 4) interaction provides a favorable free energy contribution of -0.4 kcal/mol to helix stability.
  • The reversed Arg-->Trp (i, i + 4) orientation yields no significant free energy gain.
  • Tryptophan-arginine interactions are stronger than phenylalanine-arginine interactions.
  • Cation-pi interactions showed minimal sensitivity to salt screening.

Conclusions:

  • The orientation and spacing of residues are critical for favorable cation-pi interactions in peptides.
  • Tryptophan-arginine cation-pi interactions significantly contribute to helix stability, more so than phenylalanine-arginine.
  • Experimental findings align with theoretical predictions regarding the relative strength of Trp vs. Phe in cation-pi interactions, though magnitudes differ.