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Related Concept Videos

Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Cotranslational Protein Translocation01:20

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Sec61 channel partners for cotranslational translocation
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Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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Rab Proteins

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Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
09:33

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

Surface-tethered protein switches.

Maya Zayats1, Manu Kanwar, Marc Ostermeier

  • 1Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD 21218, USA.

Chemical Communications (Cambridge, England)
|February 19, 2011
PubMed
Summary
This summary is machine-generated.

Engineered protein switches, which link input signals to output functions, have been successfully demonstrated on surfaces. This innovation presents a potential pathway toward developing a universal biosensing platform.

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Published on: January 11, 2017

Area of Science:

  • Biotechnology
  • Molecular Engineering
  • Biosensor Development

Background:

  • Protein switches are engineered fusion proteins comprising an input domain sensing a signal and an output domain whose function is modulated by the input domain's state.
  • Current biosensing technologies often require complex sample preparation and are limited in their universality.

Purpose of the Study:

  • To engineer and demonstrate a fully functional surface-tethered protein switch.
  • To explore the potential of this engineered protein switch as a component of a universal biosensing platform.

Main Methods:

  • Design and construction of fusion proteins incorporating input and output domains.
  • Surface tethering of the engineered protein switches.
  • Functional characterization of the surface-tethered protein switches in response to specific input signals.

Main Results:

  • Demonstration of a fully functional surface-tethered protein switch.
  • The engineered protein switch successfully responded to its designated input signal, modulating the output domain's function.
  • The surface-tethered format proved viable for protein switch operation.

Conclusions:

  • Surface-tethered protein switches are feasible and functional.
  • This engineered system offers a promising foundation for a universal biosensing platform.
  • Further development could lead to novel diagnostic and detection tools.