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Related Concept Videos

Mechanical Protein Functions01:58

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
Mechanical Protein Function01:58

Mechanical Protein Function

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
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.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: Jun 23, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Controlling proteins through molecular springs.

Giovanni Zocchi1

  • 1Department of Physics and Astronomy, University of California Los Angeles, Los Angeles, CA 90095-1547, USA. zocchi@physics.ucla.edu

Annual Review of Biophysics
|May 7, 2009
PubMed
Summary

Mechanical control of proteins, or mechanochemistry, is a fascinating field. This study explores using DNA molecular springs to apply controlled stress to proteins, advancing our understanding of artificial devices and natural allostery.

Area of Science:

  • Biophysics
  • Biochemistry
  • Molecular Biology

Background:

  • The mechanical control of proteins, known as mechanochemistry, offers a unique approach to understanding and manipulating biological processes.
  • Existing research has laid the groundwork for exploring how physical forces can influence protein function and chemical reactions.

Purpose of the Study:

  • To investigate the conceptual interest and current state of protein mechanochemistry.
  • To introduce and detail a novel approach using DNA molecular springs for controlled protein stress application.
  • To elucidate the underlying physical principles governing both artificial mechanochemical systems and natural allosteric mechanisms.

Main Methods:

  • Review of existing accomplishments in protein mechanochemistry.
  • Development and application of DNA molecular springs to exert controlled mechanical stress on proteins.

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Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy
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Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy

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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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  • Analysis of physical principles relevant to artificial mechanochemical devices and biological allostery.
  • Main Results:

    • Demonstration of DNA molecular springs as a viable tool for applying controlled stress to proteins.
    • Identification of key physical principles governing protein mechanochemical interactions.
    • Insights into the relationship between mechanical forces and protein allosteric regulation.

    Conclusions:

    • Protein mechanochemistry is a conceptually significant area with growing practical applications.
    • DNA molecular springs provide a powerful platform for studying protein mechanics and allostery.
    • Understanding the physical principles of mechanochemistry can bridge the gap between artificial devices and natural biological systems.