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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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Mechanical Protein Function

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Related Experiment Video

Updated: May 10, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

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Published on: April 2, 2015

Hofmeister ions control protein dynamics.

Balázs Szalontai¹, Gergely Nagy, Sashka Krumova

¹Institute of Biophysics, Biological Research Centre of the Hungarian Academy of Sciences, H-6726 Szeged, Hungary. szalontai.balazs@brc.mta.hu

Biochimica Et Biophysica Acta

|June 11, 2013

Summary

This summary is machine-generated.

Hofmeister ions influence protein dynamics by altering interfacial tension. This study experimentally validates a thermodynamic theory, showing how kosmotropic and chaotropic anions control protein conformational fluctuations.

Keywords:

Bacteriorhodopsin Differential scanning calorimetry Fourier transform infrared spectroscopy Hofmeister effect Neutron scattering Protein structural fluctuation

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Area of Science:

Biophysics
Physical Chemistry

Background:

A thermodynamic theory explains Hofmeister ion effects on proteins using interfacial tension.
The theory predicts altered protein conformational fluctuations with Hofmeister salt addition.

Purpose of the Study:

To experimentally test the thermodynamic theory's predictions regarding Hofmeister ion effects on protein dynamics.
To investigate how Hofmeister salts influence conformational fluctuations in bacteriorhodopsin.

Main Methods:

Utilized neutron scattering, micro-calorimetry, and Fourier-transform infrared spectroscopy.
Applied methods sensitive to changes in protein fluctuations.

Main Results:

Hofmeister salts modulate protein-water interfacial properties, controlling conformational fluctuations in bacteriorhodopsin.
Kosmotropic anions (COOCH3(-)) increased fluctuations below the α(II)→α(I) transition, while chaotropic anions (ClO4(-)) increased them above.
Enhanced equilibrium fluctuations preceded the thermotropic phase transition.

Conclusions:

Experimental results align with the thermodynamic theory.
Protein-water interfacial tension changes successfully predict Hofmeister effects on protein dynamics.
This framework aids understanding of protein interfacial properties and conformational dynamics.