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Peptide Bonds02:43

Peptide Bonds

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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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Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

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The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
Chymotrypsin is a pancreatic enzyme that breaks down proteins during digestion....
21.7K
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

5.2K
The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
 
Most enzymes...
5.2K
Reduction of Alkenes: Catalytic Hydrogenation02:13

Reduction of Alkenes: Catalytic Hydrogenation

14.2K
Alkenes undergo reduction by the addition of molecular hydrogen to give alkanes. Because the process generally occurs in the presence of a transition-metal catalyst, the reaction is called catalytic hydrogenation.
Metals like palladium, platinum, and nickel are commonly used in their solid forms — fine powder on an inert surface. As these catalysts remain insoluble in the reaction mixture, they are referred to as heterogeneous catalysts.
The hydrogenation process takes place on the...
14.2K
Protein Complex Assembly02:41

Protein Complex Assembly

16.9K
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...
16.9K
Reduction of Benzene to Cyclohexane: Catalytic Hydrogenation01:28

Reduction of Benzene to Cyclohexane: Catalytic Hydrogenation

5.9K
Unlike the easy catalytic hydrogenation of an alkene double bond, hydrogenation of a benzene double bond under similar reaction conditions does not take place easily. For example, in the reduction of stilbene, the benzene ring remains unaffected while the alkene bond gets reduced. Hydrogenation of an alkene double bond is exothermic and a favorable process. In contrast, to hydrogenate the first unsaturated bond of benzene, an energy input is needed; that is, the process is endothermic. This is...
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Related Experiment Video

Updated: Feb 12, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

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

Published on: November 21, 2013

13.5K

Catalytic peptide assemblies.

O Zozulia1, M A Dolan, I V Korendovych

  • 1Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA. ikorendo@syr.edu.

Chemical Society Reviews
|March 30, 2018
PubMed
Summary
This summary is machine-generated.

Short peptides self-assemble into catalytic structures. These peptide catalysts exhibit remarkable efficiency, rivaling natural enzymes, and are developed using various rational design strategies.

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Area of Science:

  • Molecular self-assembly
  • Biocatalysis
  • Peptide chemistry

Background:

  • Molecular self-assembly leads to novel emergent properties.
  • Short peptides can form diverse structures with unique physical characteristics.
  • Many peptide assemblies demonstrate significant catalytic activity, comparable to natural enzymes.

Purpose of the Study:

  • To review strategies for designing self-assembled peptide catalysts.
  • To explore the use of natural and unnatural peptide backbones.
  • To discuss the incorporation of metal-containing cofactors.

Main Methods:

  • Review of rational design strategies for peptide self-assembly.
  • Analysis of peptide backbone modifications (natural and unnatural).
  • Investigation of metal-cofactor integration in peptide assemblies.

Main Results:

  • Peptide self-assembly yields structures with tunable properties.
  • Self-assembled peptide catalysts achieve high catalytic efficiencies.
  • Design strategies enable the creation of potent artificial enzymes.

Conclusions:

  • Rational design is key to developing efficient self-assembled peptide catalysts.
  • Peptide-based catalysts offer a promising alternative to natural enzymes.
  • Future research can focus on diverse backbones and cofactor integration for enhanced catalysis.