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Related Experiment Video

Updated: Jul 15, 2026

Method to Measure Tone of Axial and Proximal Muscle

Method to Measure Tone of Axial and Proximal Muscle

Published on: December 14, 2011

Peptide pinwheels.

David T Kaleta¹, Martin F Jarrold

¹Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, USA.

Journal of the American Chemical Society

|February 14, 2002

Summary

Peptide multimers formed by electrospraying adopt stable helical arrangements. These structures, including dimers and trimers of acetylated glycine-alanine peptides with lysine, are cooperatively stabilized by electrostatic interactions.

Area of Science:

Biophysical Chemistry
Computational Chemistry
Molecular Biophysics

Background:

Peptide self-assembly and multimerization are crucial in biological systems.
Understanding the gas-phase conformations of peptide multimers provides insights into their fundamental interactions.

Purpose of the Study:

To investigate the conformations of unsolvated peptide dimers and trimers formed via electrospraying.
To elucidate the stabilizing forces governing these peptide multimers.

Main Methods:

Electrospraying of acetylated glycine-alanine peptides containing lysine.
Ion mobility measurements to probe gas-phase structures.
Molecular dynamics simulations to model and analyze conformations.

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Last Updated: Jul 15, 2026

Method to Measure Tone of Axial and Proximal Muscle

Method to Measure Tone of Axial and Proximal Muscle

Published on: December 14, 2011

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Magnetically Induced Rotating Rayleigh-Taylor Instability

Published on: March 3, 2017

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Main Results:

Electrospraying produced significant signals for unsolvated peptide dimers and trimers.
Peptide trimers adopt a pinwheel arrangement of helices, stabilized by lysine side chains and helix dipoles.
Peptide dimers form a V-shaped helical structure, also exhibiting cooperative electrostatic stabilization.

Conclusions:

The study reveals specific, stable helical arrangements for peptide dimers and trimers in the gas phase.
Cooperative electrostatic interactions, particularly involving lysine side chains and helix dipoles, are key to multimer stability.
Ion mobility and molecular dynamics are effective tools for characterizing peptide multimer structures.