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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...

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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

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Energy to Drive Translocation

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

Protein Organization

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: Dec 30, 2025

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

Electron Transfer across Helical Peptides.

Nadav Amdursky¹

¹Departments of Materials and Bioengineering, Imperial College London, London SW7 2AZ (UK).

|January 25, 2020

Summary

This summary is machine-generated.

Electron transfer across alpha-helical peptides is crucial for bioelectronic devices. This review discusses methods like photoinduced electron transfer and electrochemistry to understand and control this process.

Keywords:

electron transfer electron transport peptides photochemistry protein structures

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Last Updated: Dec 30, 2025

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

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Published on: August 20, 2018

Area of Science:

Biophysics
Materials Science
Biochemistry

Background:

Electron transfer (ET) is fundamental in biological systems.
Alpha-helical peptides are promising for bioelectronic devices due to their structure and ease of modification.

Purpose of the Study:

To review and discuss methodologies for studying ET across alpha-helical peptides.
To explore functionalization strategies for controlling optoelectronic properties.

Main Methods:

Photoinduced electron transfer (ET).
Electrochemistry.
Solid-state conductivity measurements (electron transport, ETp).

Main Results:

Compares fundamental differences between ET methodologies.
Discusses appropriate result interpretation and potential mechanisms for ET(p).
Reviews peptide functionalization for tuning electronic properties.

Conclusions:

Alpha-helical peptides are key for bioelectronic applications.
Understanding ET mechanisms across these peptides is vital for device development.
Functionalization offers a route to tailor peptide optoelectronic performance.