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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Crowding induced self-assembly and enthalpy-entropy compensation.

Jack F Douglas1, Jacek Dudowicz, Karl F Freed

  • 1Polymers Division, National Institute of Standards and Technology, Gaithersburg, Maryland 20899, USA.

Physical Review Letters
|November 13, 2009
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Summary

Molecular additives influence protein self-assembly. A specific temperature, T_{Theta}, marks an enthalpy-entropy balance where polymer-protein interactions optimize assembly stability.

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Area of Science:

  • Biophysics
  • Physical Chemistry
  • Materials Science

Background:

  • Self-assembly of proteins and molecular species is crucial in biological systems and materials science.
  • Understanding the impact of additives, such as polymers, on self-assembly is key to controlling these processes.

Purpose of the Study:

  • To develop a theoretical framework describing how molecular additives affect the equilibrium self-assembly of proteins or other molecular species.
  • To investigate the specific role of high molar mass polymer additives and identify conditions for optimal self-assembly.

Main Methods:

  • Development of a general virial expansion to model the interactions between molecular additives and self-assembling species (M).
  • Specialization of the virial expansion for high molar mass polymer additives.
  • Analysis of the cross-virial coefficient to determine its behavior and significance.

Main Results:

  • The cross-virial coefficient between polymer additives and species M dictates the influence on self-assembly.
  • This coefficient vanishes at a specific temperature, T_{Theta}, indicating an enthalpy-entropy compensation point.
  • Repulsive polymer-protein interactions initially enhance assembly stability by modifying entropy, but this is counteracted by attractive interactions affecting enthalpy.

Conclusions:

  • A general virial expansion provides a robust method for predicting the effects of molecular additives on self-assembly.
  • The identified temperature T_{Theta} represents a critical point where opposing enthalpic and entropic contributions balance, optimizing the stability of the assembled state.
  • This work offers insights into controlling protein and molecular self-assembly through tailored additive design.