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Related Concept Videos

Protein Denaturation01:28

Protein Denaturation

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The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
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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.
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Mechanical Protein Functions01:58

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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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Induced Electric Fields01:23

Induced Electric Fields

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The fact that emfs are induced in circuits implies that work is being done on the conduction electrons in the wires. What can possibly be the source of this work? We know that it’s neither a battery nor a magnetic field, as a battery does not have to be present in a circuit where current is induced, and magnetic fields never do any work on moving charges. The source of the work is in fact an electric field that is induced in the wires. For example, if a stationary conductor is placed in a...
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Molecular Chaperones and Protein Folding03:00

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Related Experiment Video

Updated: May 2, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
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Electric field induced changes in protein conformation.

Innocent Bekard1, Dave E Dunstan

  • 1CSL Behring, 189-209 Camp Road, Broadmeadows, Victoria, 3047, Australia.

Soft Matter
|March 22, 2014
PubMed
Summary

Low strength oscillating electric fields cause protein unfolding in Bovine Serum Albumin (BSA) and Lysozyme. Electrophoretic motion generates frictional forces, leading to unfolding and potential aggregation.

Area of Science:

  • Biophysics
  • Protein Chemistry

Background:

  • Proteins like Bovine Serum Albumin (BSA) and Lysozyme are crucial in biological systems.
  • Understanding protein conformation changes is vital for comprehending biological functions and diseases.

Purpose of the Study:

  • To investigate the impact of low-strength oscillating electric fields on the conformation of BSA and Lysozyme.
  • To elucidate the mechanism by which electric fields induce protein unfolding.

Main Methods:

  • Utilized a custom-built cell to monitor real-time autofluorescence and Circular Dichroism.
  • Applied oscillating electric fields of varying strengths and frequencies to protein solutions.

Main Results:

  • Observed protein unfolding in both BSA and Lysozyme upon exposure to electric fields.

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  • Proposed a model where electrophoretic motion induces frictional forces, causing unfolding.
  • Quantified shear rates at protein surfaces during electrophoretic motion.

    • Conclusions:

    • Low-strength electric fields can induce protein unfolding through electrophoretic motion and frictional dissipation.
    • Protein unfolding is a potential initial step in protein aggregation and amyloid formation.