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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:

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Related Experiment Video

Updated: May 10, 2026

The Use of a &#946;-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions
08:06

The Use of a β-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions

Published on: February 1, 2018

An engineered calmodulin-based allosteric switch for Peptide biosensing.

Glenna E Meister1, Neel S Joshi

  • 1School of Engineering and Applied Sciences, Harvard University, 29 Oxford Street, Cambridge, MA 02143, USA.

Chembiochem : a European Journal of Chemical Biology
|July 5, 2013
PubMed
Summary
This summary is machine-generated.

Researchers engineered a novel allosteric protein switch using calmodulin and TEM1 β-lactamase. This biosensor platform demonstrates ligand-dependent control over enzyme activity, enabling potential applications in biomarker detection.

Keywords:
allosterybiosensorscalmodulindomain insertionprotein engineering

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The Use of a &#946;-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions
08:06

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Published on: February 1, 2018

Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions
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Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions

Published on: December 1, 2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Calmodulin undergoes conformational changes upon ligand binding.
  • Protein engineering aims to create novel functional proteins.
  • Allosteric regulation involves conformational changes affecting protein activity.

Purpose of the Study:

  • To develop a new platform for allosteric protein engineering.
  • To create a fusion protein where calmodulin controls enzyme activity.
  • To establish a versatile scaffold for biosensor development.

Main Methods:

  • Genetically fusing calmodulin to TEM1 β-lactamase.
  • Utilizing calmodulin's ligand-dependent conformational changes.
  • Measuring the catalytic activity of the fusion protein in vitro.

Main Results:

  • The engineered allosteric enzyme showed up to 120-fold increase in activity upon peptide binding.
  • Enzyme activation was dependent on peptide affinity for calmodulin.
  • The system demonstrated ligand-controlled modulation of enzyme function.

Conclusions:

  • The calmodulin-β-lactamase fusion protein serves as a functional allosteric switch.
  • This platform is a promising scaffold for directed evolution of biosensors.
  • Potential applications include detecting toxins and clinical biomarkers.