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Related Concept Videos

Protein Folding01:25

Protein Folding

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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
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ATP and Macromolecule Synthesis01:28

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Biological macromolecules are organic compounds, predominantly composed of carbon atoms. The carbon atoms are covalently bonded with hydrogen, oxygen, nitrogen, and other minor elements. There are four major biological macromolecule classes: carbohydrates, lipids, proteins, and nucleic acids.
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Protein Complex Assembly02:41

Protein Complex Assembly

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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.
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Conservation of Protein Domains Over Different Proteins02:26

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Molecular Chaperones and Protein Folding03:00

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
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Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

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[Advances in protein cyclization].

Xinzhe Wang1, Guangya Zhang1

  • 1Department of Bioengineering and Biotechnology, Huaqiao University, Xiamen 361021, Fujian, China.

Sheng Wu Gong Cheng Xue Bao = Chinese Journal of Biotechnology
|August 31, 2017
PubMed
Summary
This summary is machine-generated.

Protein cyclization enhances enzyme stability for industrial applications. This review covers traditional methods and a novel SpyTag/SpyCatcher approach for creating stable cyclic enzymes.

Keywords:
SpyTag/SpyCatcherexpressed protein ligationphotocontrol inteinprotein trans-splicingsortase-catalyzed transpeptidation

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Area of Science:

  • Biochemistry
  • Protein Engineering

Background:

  • Proteins, primarily linear in vivo, exhibit limited stability against temperature and pH changes.
  • This instability restricts the use of enzymes in industrial catalysis, food manufacturing, and medicine.
  • Natural cyclic peptides possess inherent thermal stability, offering a model for enhancing protein stability.

Purpose of the Study:

  • To review advancements in protein cyclization techniques.
  • To explore methods for improving enzyme thermal stability and structural modification.
  • To detail a novel SpyTag/SpyCatcher-mediated enzyme cyclization strategy.

Main Methods:

  • Review of existing literature on protein cyclization.
  • Summary of traditional methods: protein trans-splicing, expressed protein ligation, and sortase-catalyzed transpeptidation.
  • Detailed discussion of SpyTag/SpyCatcher-mediated enzyme cyclization.

Main Results:

  • Protein cyclization is a viable strategy to improve enzyme stability.
  • Traditional methods offer established routes for protein cyclization.
  • SpyTag/SpyCatcher system presents a novel and efficient method for enzyme cyclization.

Conclusions:

  • Enzyme cyclization significantly enhances thermal stability and broadens application scope.
  • The SpyTag/SpyCatcher system provides a promising new avenue for protein engineering.
  • Further research into protein cyclization will unlock new biotechnological applications.