Related Experiment Video
Updated: Nov 25, 2025
05:08
Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
Published on: July 8, 2025
667
Development and applications of artificial symmetrical proteins
Jeroen P M Vrancken1, Jeremy R H Tame2, Arnout R D Voet1
1Laboratory of Biomolecular Modelling and Design, Department of Chemistry, KU Leuven, Celestijnenlaan 200G, 3001 Leuven, Belgium.
Computational and Structural Biotechnology Journal
|December 18, 2020
Summary
Artificial protein design has advanced significantly, enabling the creation of novel symmetrical proteins from repeating units. This review explores their design principles and diverse applications in chemistry and medicine.
Area of Science:
- Biochemistry
- Protein Engineering
- Synthetic Biology
Background:
- Interest in artificial protein creation dates back to early molecular models.
- Recent decades have seen significant advancements in protein design methodologies.
- Many successful artificial proteins incorporate repetitive structural elements.
Purpose of the Study:
- To review the design strategies for artificial symmetrical proteins.
- To highlight the diverse applications of these engineered proteins.
- To provide an overview of recent progress in the field.
Main Methods:
- Review of existing literature on protein design.
- Analysis of methods for constructing symmetrical protein architectures.
- Compilation of examples of non-natural protein applications.
Main Results:
- Numerous examples of de novo designed proteins exist.
- Symmetrical protein designs are frequently based on repeating units.
- These proteins have demonstrated utility in various chemical and medical contexts.
Conclusions:
- Artificial protein design, particularly for symmetrical structures, is a rapidly advancing field.
- Engineered symmetrical proteins offer versatile platforms for chemical and medical innovations.
- Continued research promises further expansion of their applications.
Related Concept Videos
01:22Protein Folding
124.8K
Overview
124.8K
01:25Protein Folding
10.2K
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 Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
10.2K
02:26Conservation of Protein Domains Over Different Proteins
13.7K
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.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
13.7K
02:15Protein and Protein Structure
84.8K
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...
A protein's shape is critical to its function. For example, an enzyme...
84.8K
03:03Amyloid Fibrils
11.2K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
11.2K
01:58Mechanical Protein Functions
5.3K
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force.
5.3K