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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.
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Related Experiment Video

Updated: May 21, 2026

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase

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Published on: September 26, 2020

Conformational selection in trypsin-like proteases.

Nicola Pozzi¹, Austin D Vogt, David W Gohara

¹Edward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, MO 63104, United States.

Current Opinion in Structural Biology

|June 6, 2012

Summary

This summary is machine-generated.

Protein allostery is explained by conformational selection, not just induced-fit. This finding impacts drug design and reveals trypsin-like proteases exist in two distinct forms, E and E*, enabling new therapeutic applications.

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The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Area of Science:

Biochemistry
Structural Biology
Pharmacology

Background:

Protein allostery has been interpreted through two main mechanisms: conformational selection and induced-fit.
Understanding these mechanisms is crucial for developing effective drugs and therapeutics.
Trypsin-like proteases are key enzymes with implications in various biological processes.

Purpose of the Study:

To investigate the mechanism of ligand recognition in trypsin-like proteases.
To elucidate the role of conformational selection in protein allostery.
To explore the therapeutic potential of understanding protease allosteric mechanisms.

Main Methods:

Kinetics studies to analyze enzyme activity and conformational states.
Structural database analysis to confirm protein conformations.
Allosteric modeling to interpret experimental data.

Main Results:

Trypsin-like proteases exist in an equilibrium between an active, substrate-accessible form (E) and an inactive, occluded form (E*).
Structural data confirm the existence of both E and E* forms, supporting the allosteric nature of the trypsin fold.
Conformational selection is demonstrated as a key mechanism in trypsin-like protease allostery.

Conclusions:

Conformational selection provides a new paradigm for understanding protease allostery.
This understanding enables protein engineers to develop novel protease-based therapeutics.
The findings have significant implications for drug design and enzyme engineering.