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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...

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 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.

Protein Organization

Protein Organization

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Peptidoglycan Synthesis

Peptidoglycan Synthesis

Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan biosynthesis begins in...

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Related Experiment Video

Updated: May 14, 2026

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

A robust route to enzymatically functional, hierarchically self-assembled peptide frameworks.

S Sangiambut¹, K Channon, N M Thomson

¹Biological and Soft Systems, Cavendish Laboratory, University of Cambridge, CB3 0HE, UK.

Advanced Materials (Deerfield Beach, Fla.)

|January 24, 2013

Summary

This summary is machine-generated.

Researchers developed a novel method to attach enzymes to peptide nanofibers, creating a biopolyester coating for medical applications. This functionalization enhances self-assembling peptide nanofibers without compromising their structure.

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Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

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Last Updated: May 14, 2026

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

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

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Area of Science:

Biomaterials Science
Nanotechnology
Biochemistry

Background:

Integrating enzyme biofunctionality into self-assembling peptide nanofibers is difficult.
Enzyme addition can disrupt fiber self-assembly and impair enzyme activity.

Purpose of the Study:

To develop a robust method for enzyme functionalization of peptide nanofibers.
To create functional bionanomaterials for medical engineering applications.

Main Methods:

Demonstrated a novel peptide nanofiber enzyme functionalization technique.
Attached a polymerization synthase enzyme to peptide nanofibers.

Main Results:

Successfully generated a biocompatible and biodegradable biopolyester coat on the peptide nanofibers.
The functionalization method preserved the self-assembly properties of the nanofibers.

Conclusions:

The developed method enables the creation of functional bionanomaterials by enzyme-coating peptide nanofibers.
This approach offers a versatile template for designing advanced biomaterials for medical engineering.