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

Protein Folding

Protein Folding

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...

Protein Folding

Protein Folding

Protein Organization

Protein Organization

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...

Peptide Bonds

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...

You might also read

Related Articles

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

Sort by

Same author

Morphology Assessment Enabled by Room-Temperature Soft-Landing in Native MS.

International journal of mass spectrometry·2026

Same author

Interface Architecture of a VHL-PROTAC Complex with and without Cullin-2.

Journal of the American Chemical Society·2026

Same author

Mechanism of single-strand annealing from native mass spectrometry and cryo-EM structures of RAD52 homolog Mgm101.

Nucleic acids research·2026

Same author

Damaging the conical morphology of HIV-1 capsid by targeting the FG-binding pocket and disfavoring pentameric subunits needed for core closure.

bioRxiv : the preprint server for biology·2026

Same author

Efficient tag-less purification of recombinant human tau proteins.

Analytical biochemistry·2026

Same author

Ion Mobility Mass Spectrometry Guided Modeling with AlphaFold and Rosetta Improves Protein Complex Structure Prediction.

bioRxiv : the preprint server for biology·2026

Same journal

Decoding Galectin-Glycan Recognition with <sup>19</sup>F-Tagged Lectins: from Simple Glycans to the Cellular Glycocalyx.

Journal of the American Chemical Society·2026

Same journal

Open- and Closed-Shell Roles of Sensitizer and Annihilator in Pseudo-Single Component Mixtures for Upconversion.

Journal of the American Chemical Society·2026

Same journal

Pressure-Induced Superconductivity at 15 K in van-der-Waals Ferroelectric CuInP<sub>2</sub>S<sub>6</sub>.

Journal of the American Chemical Society·2026

Same journal

Carbene Analogues of Group 15: Reduction of s-Hydrindacene-Based Chloropnictogenium Ions To Access an Antimony Hydride Monocation and a Trinuclear Bismuth Dication.

Journal of the American Chemical Society·2026

Same journal

Chiral-Ligand-Modulated Nickel-Catalyzed Stereoselective Radical Migratory C2-Arylation of Carbohydrates.

Journal of the American Chemical Society·2026

Same journal

Coordination-Constraint-Driven Enhanced Chirality Induction in Perovskite Quantum Dot Solids.

Journal of the American Chemical Society·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Apr 24, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Gas-phase helical peptides mimic solution-phase behavior.

Lindsay J Morrison¹, Vicki H Wysocki

¹Ohio State University , 484 West 12th Avenue, Columbus, Ohio 43210, United States.

Journal of the American Chemical Society

|September 10, 2014

Summary

This summary is machine-generated.

Gas-phase peptide studies reveal alpha-helix stabilization at termini. Helical and globular conformations of doubly charged peptides were analyzed, showing sequence and length influence stability.

More Related Videos

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

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

Published on: August 1, 2018

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility

Published on: September 6, 2024

Related Experiment Videos

Last Updated: Apr 24, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

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

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

Published on: August 1, 2018

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility

Published on: September 6, 2024

Area of Science:

Biophysical Chemistry
Mass Spectrometry
Protein Conformation

Background:

Alpha-helices in solution are stabilized by terminal capping interactions.
Gas-phase studies offer insights into intrinsic stabilizing properties.
Previous solution-phase studies examined N-terminal amino acid effects.

Purpose of the Study:

To investigate helical and globular conformations of gas-phase peptides.
To explore the influence of peptide sequence and length on helical stability.
To analyze the conformational preferences of peptide fragments.

Main Methods:

Analysis of gas-phase, doubly charged peptides (XAnK).
Mass spectrometry to study peptide conformations and fragmentation.
Varying collision energies to induce conformational changes.

Main Results:

Helical and globular conformations observed in gas-phase peptides.
Helical conformation abundance depends on peptide length and N-terminal residue (X).
Helical b-ion fragments preferentially form at lower collision energies, especially from helical precursors.

Conclusions:

Gas-phase peptide studies confirm solution-phase observations on helical stabilization.
Fragment stability is influenced by length, N-terminal residue, precursor conformation, and collision energy.
A minimum fragment length (b10) is required for stable helical conformations in b-ions.