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Related Experiment Video

Updated: Jun 12, 2026

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

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

Published on: November 21, 2013

Molecular self-assembly in a model amphiphile system.

Lorna Dougan¹, Jason Crain, John L Finney

¹School of Physics and Astronomy, University of Leeds, Leeds, LS2 9JT, UK. L.Dougan@leeds.ac.uk

Physical Chemistry Chemical Physics : PCCP

|June 12, 2010

Summary

The excess entropy of mixing alcohols and water is explained by molecular demixing, not water structuring. Changes in cluster topology under cold and pressure conditions offer insights into protein denaturation.

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Area of Science:

Physical Chemistry
Biophysics

Background:

The origin of negative excess entropy in alcohol-water mixtures is debated.
Standard explanations involve water structuring, but recent studies suggest molecular-scale demixing.

Purpose of the Study:

To investigate the negative excess entropy (DeltaS(E)) of aqueous methanol at low temperatures and high pressures.
To explore the role of molecular self-assembly and cluster topology in these mixtures.

Main Methods:

Utilized experimentally-derived structural data.
Employed a recently introduced cluster model to estimate DeltaS(E).

Main Results:

Cooling to 190 K increased cluster sizes but did not significantly alter DeltaS(E), indicating topological changes.
Compression increased cluster sizes and resulted in a positive DeltaS(E), suggesting pronounced topological shifts.
The amphiphilic nature of molecules drives aggregation and self-assembly in aqueous solutions.

Conclusions:

The study highlights the importance of molecular amphiphilicity in self-assembly processes.
Findings provide insights into cold and pressure denaturation mechanisms in proteins.