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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
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 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...
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...
Protein Organization01:13

Protein Organization

Overview
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.

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Related Experiment Video

Updated: Jul 10, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

beta-sheet hydrogen bonding patterns in cystine peptides.

Timothy J Cashman1, Brian R Linton

  • 1Department of Chemistry, Bowdoin College, Brunswick, Maine 04011, USA.

Organic Letters
|November 23, 2007
PubMed
Summary

Cystine peptides in organic solvents mimic beta-sheet structures. Hydrogen/deuterium exchange revealed hydrogen bond strengths and aggregation in these peptide conformations.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Peptide Chemistry

Background:

  • Cystine peptides are known to form specific conformations in solution.
  • Beta-sheet structures are crucial in protein folding and function.

Purpose of the Study:

  • To investigate the conformational behavior of cystine peptides in organic solvents.
  • To elucidate the role of hydrogen bonding in stabilizing these structures.

Main Methods:

  • Utilized hydrogen/deuterium exchange techniques.
  • Analyzed peptide aggregation and hydrogen bond characteristics.

Main Results:

  • Cystine peptides adopt beta-sheet-like conformations in organic solvents.
  • Identified relative hydrogen bond strengths and specific donor/acceptor identities.

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

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  • Characterized beta-strand aggregation patterns.

    • Conclusions:

    • Conformations of cystine peptides in organic solvents resemble small beta-sheets.
    • Hydrogen/deuterium exchange is effective in detailing hydrogen bonding and aggregation in peptides.