Related Experiment Video
Updated: Jun 4, 2026
08:50
High-Speed Magnetic Tweezers for Nanomechanical Measurements on Force-Sensitive Elements
Published on: May 12, 2023
Knitting and snipping: chaperones in β-helix folding
1Department of Molecular Structural Biology, Institute for Microbiology and Genetics, Georg-August-University Goettingen, Justus-von-Liebig-Weg 11, 37077 Goettingen, Germany.
Current Opinion in Structural Biology
|February 19, 2011
Summary
Beta-helical proteins are stable but prone to aggregation. Specialized chaperones aid triple beta-helix assembly, with recent studies revealing two distinct chaperone classes for tailspike protein maturation.
Area of Science:
- Protein folding and assembly
- Structural biology
- Biochemistry
Background:
- Beta-helical proteins exhibit high stability and rigidity.
- Their folding pathways are prone to aggregation.
- Triple beta-helices often require specific signals or chaperones for correct assembly.
Purpose of the Study:
- To elucidate the structural and mechanistic basis of intramolecular chaperone action in beta-helical protein assembly.
- To compare the mechanisms of two distinct classes of chaperones involved in tailspike protein maturation.
Main Methods:
- X-ray crystallography was used to determine the structures of two classes of intramolecular chaperones.
- Analysis of protein structures to understand chaperone-mediated assembly and autoproteolytic release.
Main Results:
- Crystal structures of two classes of intramolecular chaperones for beta-helical proteins were determined.
- Both chaperone classes mediate the assembly of large tailspike proteins.
- The two chaperone classes exhibit significant differences in their structures and autoproteolytic release mechanisms.
Conclusions:
- Intramolecular chaperones play crucial roles in the proper folding and assembly of complex beta-helical proteins like tailspikes.
- Understanding these chaperone mechanisms provides insights into protein maturation and quality control.
- Distinct structural and functional strategies exist for chaperone-mediated protein assembly and release.
Related Concept Videos
03:00Molecular 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.
The...
The...
03:00Molecular 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.
The...
The...
01:25Protein 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 Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
01:22Protein Folding
Overview
01:22Protein Folding
Overview
01:26Bacterial Protein Maturation
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...