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Related Concept Videos

Microbial Biosensors01:17

Microbial Biosensors

Microbial biosensors are analytical devices that utilize living microbes to detect specific substances through measurable signals. These devices consist of two main components: biosensing organisms and signal-transducing elements. Biosensing organisms, such as Escherichia coli or Saccharomyces cerevisiae, are typically housed in multiwell plates connected to transducers, enabling rapid, real-time detection of target analytes.Signal Generation MechanismWhen a target analyte—such as...
Riboswitches01:56

Riboswitches

Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...

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Related Experiment Video

Updated: Jun 6, 2026

Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy
12:24

Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy

Published on: September 29, 2016

Converting a protein into a switch for biosensing and functional regulation.

Margaret M Stratton1, Stewart N Loh

  • 1Department of Biochemistry and Molecular Biology, State University of New York Upstate Medical University, 750 East Adams Street, Syracuse, New York 13210, USA.

Protein Science : a Publication of the Protein Society
|November 11, 2010
PubMed
Summary

Researchers engineer proteins to act as molecular switches by introducing conformational changes. This review highlights methods for converting traditional binding proteins into responsive switches for biosensor applications.

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Area of Science:

  • Biochemistry
  • Protein Engineering
  • Molecular Biology

Background:

  • Proteins that change shape upon signaling are key for reagent-free biosensors and regulated molecular functions.
  • A major challenge is that most natural proteins lack this conformational switching ability upon ligand binding or modification.

Purpose of the Study:

  • To review recent protein engineering strategies for inducing conformational switching in binding proteins.
  • To explore methods for converting static binding proteins into dynamic molecular switches.

Main Methods:

  • Co-opting natural allosteric coupling mechanisms.
  • Joining proteins through novel protein engineering approaches.
  • Developing entirely new protein switching mechanisms.

Main Results:

  • Demonstrated success in engineering proteins to exhibit conformational changes.
  • Provided insights into converting 'lock-and-key' proteins into functional molecular switches.
  • Highlighted the potential for designing novel biosensors and regulated biological molecules.

Conclusions:

  • Protein engineering offers viable strategies to create conformational switching proteins.
  • These engineered switches have significant implications for biosensor design and molecular regulation.
  • Continued research is advancing the ability to control protein conformation for technological applications.