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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

Amyloid Fibrils

Amyloid Fibrils

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, normally used to...

Amyloid Fibrils

Amyloid Fibrils

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, normally used to...

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.
The...

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Related Experiment Video

Updated: Jun 22, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

Alpha/beta hydrolase fold: an update.

Paul D Carr¹, David L Ollis

¹Research School of Chemistry, Australian Nation University, Building 35, Science Road, Canberra, ACT 0200, Australia.

Protein and Peptide Letters

|June 11, 2009

Summary

The alpha/beta hydrolase superfamily is rapidly expanding, with 89 families cataloged. This review offers a current overview of their taxonomy, chemistry, structures, and emerging technologies.

Area of Science:

Biochemistry and Molecular Biology
Enzymology

Background:

The alpha/beta hydrolase superfamily is a large and diverse group of enzymes.
Recent years have seen a significant expansion in the study and characterization of this superfamily.
The ESTHER database serves as a key resource for information on alpha/beta hydrolases.

Purpose of the Study:

To provide a comprehensive snapshot of the current state of knowledge regarding the alpha/beta hydrolase superfamily.
To detail the family taxonomy, catalytic mechanisms, and structural features.
To highlight emerging technologies and applications derived from this enzyme class.

Main Methods:

Literature review and data compilation from the ESTHER database.
Analysis of published research on alpha/beta hydrolase families, genes, and structures.

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Last Updated: Jun 22, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

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Published on: September 15, 2010

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

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Published on: May 13, 2020

Synthesis of information on catalytic chemistries and structural topologies.

Main Results:

The alpha/beta hydrolase superfamily encompasses 89 distinct family groups.
A total of 15,438 gene loci and 666 protein structures have been identified.
The review consolidates current understanding of their diverse catalytic functions and structural diversity.

Conclusions:

The alpha/beta hydrolase superfamily represents a vast and dynamic area of biochemical research.
Continued exploration yields insights into novel catalytic activities and structural motifs.
Emerging technologies leverage the unique properties of these enzymes for various applications.