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

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 Folding01:22

Protein Folding

Overview
Protein and Protein Structure02:15

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 can...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

Overview
Peptide Bonds02:43

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

Purification of post-transcriptionally modified tRNAs for enhanced cell-free translation systems.

Nucleic acids research·2026
Same author

Co-Translational Incorporation of <i>(R)</i>- and <i>(S)</i>-β<sup>2</sup>-Hydroxy Acids <i>In Vitro</i>: A Structural and Biochemical Study on the <i>E. coli</i> Ribosome.

Journal of the American Chemical Society·2026
Same author

Co-Translational Incorporation of (<i>R</i>)- and (<i>S</i>)-β<sup>2</sup>-Hydroxyacids <i>In Vivo</i>: Directed Evolution of Efficient Aminoacyl-tRNA Synthetases.

Journal of the American Chemical Society·2026
Same author

Expanding the multiplexing capability of HIDE probes via fluorescence lifetime imaging microscopy.

Methods in enzymology·2026
Same author

A clickable CoQ imaging probe reveals that cellular uptake and lysosomal trafficking depend on CD36 and NPC1.

Redox biology·2026
Same author

An archaeal genetic code with all TAG codons as pyrrolysine.

Science (New York, N.Y.)·2025
Same journal

Reaction Optimization for Enzymatic Deconstruction of Industrially Relevant Nylon Composites.

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

Deploying Artificial Metalloenzymes in Complex Environments: Strategies and Applications.

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

Synthetic Ligands of Myeloid C-Type Lectin Receptors.

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

Vancomycin-Mediated Binding of DNA Origami Nanostructures to Gram-Positive and Gram-Negative Bacteria.

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

Mutasynthesis and Antibiotic Activity of Mupirocin Analogues.

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

Pressure-Dependent Aromatic Ring Flips Reveal Variable Transition-State Volume and Compressibility Among Structural Regions of BPTI.

Chembiochem : a European journal of chemical biology·2026
See all related articles

Related Experiment Video

Updated: Jun 3, 2026

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

Enhancing β3 -peptide bundle stability by design.

Cody J Craig1, Jessica L Goodman, Alanna Schepartz

  • 1Department of Chemistry, Yale University, New Haven, CT 06520-8107, USA. alanna.schepartz@yale.edu

Chembiochem : a European Journal of Chemical Biology
|April 2, 2011
PubMed
Summary
This summary is machine-generated.

Optimizing salt bridge length in beta-peptide bundles enhances their thermodynamic stability. This research advances the bottom-up assembly of defined beta-peptide structures with potential for sophisticated functions.

More Related Videos

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

Related Experiment Videos

Last Updated: Jun 3, 2026

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

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

Area of Science:

  • Biochemistry
  • Materials Science
  • Structural Biology

Background:

  • Beta-peptides are synthetic peptides that can self-assemble into ordered structures.
  • The Zwit-1F beta-peptide bundle, an octamer, exhibits a packed core and a salt-bridge-rich surface.
  • Zwit-1F contains nonideal interhelical salt bridges with longer heavy atom distances than typical in proteins.

Purpose of the Study:

  • To investigate if optimizing salt bridge length can enhance the thermodynamic stability of beta-peptide bundles.
  • To further understand the principles governing the self-assembly of beta-peptide structures.

Main Methods:

  • Systematic modification of interhelical salt bridge lengths in the Zwit-1F beta-peptide structure.
  • Thermodynamic stability measurements of the modified beta-peptide bundles.
  • Analysis of the structural consequences of salt bridge optimization.

Main Results:

  • Optimizing the length of four specific interhelical salt bridges significantly enhanced the thermodynamic stability of the beta-peptide bundle.
  • These findings complement previous work on the importance of internal packing residues.
  • The study demonstrates a method for fine-tuning beta-peptide assembly stability.

Conclusions:

  • Salt bridge length is a critical parameter for controlling the thermodynamic stability of beta-peptide assemblies.
  • This work represents a significant step towards the rational, bottom-up design of beta-peptide structures with controlled size, reproducibility, and function.