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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. 
Protein Folding01:25

Protein Folding

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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
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. 

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Updated: May 10, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Mechanical resistance in unstructured proteins.

Sigurður Ægir Jónsson1, Simon Mitternacht, Anders Irbäck

  • 1Computational Biology & Biological Physics, Department of Astronomy and Theoretical Physics, Lund University, Lund, Sweden.

Biophysical Journal
|June 25, 2013
PubMed
Summary
This summary is machine-generated.

Unstructured proteins like amyloid beta and alpha-synuclein resist pulling forces due to structures resembling amyloid fibrils. This finding offers insights into neurodegenerative disease mechanisms.

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Area of Science:

  • Biophysics
  • Neuroscience
  • Structural Biology

Background:

  • Single-molecule pulling experiments reveal high rupture forces for unstructured proteins linked to neurodegenerative diseases.
  • These forces are unexpectedly comparable to those of stable folded proteins, prompting investigation into underlying structural mechanisms.

Purpose of the Study:

  • To investigate the structural mechanisms behind the force resistance of amyloid beta-peptide (Aβ) and α-synuclein (αS).
  • To analyze the conformations of Aβ and αS that lead to high rupture forces in pulling simulations.

Main Methods:

  • Pulling simulations of Aβ and αS were performed, starting from simulated conformational ensembles of free monomers.
  • Analysis focused on protein conformations immediately preceding rupture events.

Main Results:

  • Simulations successfully reproduced experimental rupture events for Aβ and αS.
  • Mechanically resistant structures share a common architecture, similar to amyloid fibril folds.
  • The Arctic mutation in Aβ increased the occurrence of highly force-resistant structures.

Conclusions:

  • High rupture forces in Aβ and αS pulling experiments are attributed to specific protein structures.
  • These force-resistant structures may play a crucial role in amyloid formation.
  • The findings provide a structural basis for understanding protein behavior under mechanical stress in disease contexts.