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Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Updated: Jul 3, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

Ion specific protein assembly and hydrophobic surface forces.

Mikael Lund1, Pavel Jungwirth, Clifford E Woodward

  • 1Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic. mikael.lund@uochb.cas.cz

Physical Review Letters
|July 23, 2008
PubMed
Summary

Large anions attract hydrophobic surfaces, driving protein interactions. This ion-specific effect, observed in NaI and NaCl solutions, impacts biomolecular assembly and Hofmeister effects.

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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

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Last Updated: Jul 3, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Area of Science:

  • Physical chemistry
  • Biophysics
  • Computational chemistry

Background:

  • Ions interact differently with hydrophobic surfaces, with large anions attracted and small ions repelled.
  • These differential interactions can influence the behavior of biomolecules in solution.

Purpose of the Study:

  • To investigate ion-specific protein-protein interactions mediated by hydrophobic surface patches.
  • To quantify these interactions using computational simulations and compare with experimental data.

Main Methods:

  • Employed explicit solvent and continuum model simulations.
  • Calculated potentials of mean force for lysozyme in NaI and NaCl solutions.
  • Determined second virial coefficients to characterize protein-protein interactions.

Main Results:

  • Demonstrated significant ion-specific protein-protein interactions driven by hydrophobic patches.
  • Simulated second virial coefficients for lysozyme showed good agreement with experimental values.
  • Highlighted the role of ionic interactions with nonpolar surface groups.

Conclusions:

  • Ionic interactions with nonpolar protein groups are crucial for biomolecular assembly.
  • These findings provide insights into Hofmeister-type effects and ion-induced protein behavior.