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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 Folding

Protein Folding

Protein Folding

Protein Folding

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

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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Molecular Chaperones and Protein Folding

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Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

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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Related Experiment Video

Updated: Mar 14, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Smoothing a rugged protein folding landscape by sequence-based redesign.

Benjamin T Porebski^1,2, Shani Keleher¹, Jeffrey J Hollins³

¹Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.

Scientific Reports

|September 27, 2016

Summary

This summary is machine-generated.

Consensus design created conserpin, a synthetic serpin resistant to misfolding and aggregation. This engineered protein balances stability and function, offering a new approach for therapeutic protein development.

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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Area of Science:

Protein folding and biophysics
Molecular biology and protein engineering

Background:

Proteins with complex folding landscapes, like serine protease inhibitors (serpins), risk misfolding and aggregation.
Serpin metastability is crucial for protease inhibition but also causes misfolding diseases, such as alpha-1-antitrypsin deficiency.

Purpose of the Study:

To investigate how protein folding, function, and stability can be balanced.
To engineer a synthetic serpin with improved folding properties and resistance to aggregation.

Main Methods:

Utilized consensus design to create a synthetic serpin, termed conserpin.
Characterized conserpin's structure, folding dynamics, and stability.

Main Results:

Conserpin exhibits reversible folding, functionality, thermostability, and resistance to polymerization.
Consensus design successfully remodeled the protein's folding landscape, reconciling stability and function.
Aggregation-prone intermediates were removed, and the scaffold was modified for potential therapeutic applications.

Conclusions:

Consensus design is a viable strategy for engineering proteins with challenging folding landscapes.
Conserpin serves as a model for developing stable, functional, and aggregation-resistant protein therapeutics.