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Updated: Jul 13, 2026
10:21
Automated Hydrophobic Interaction Chromatography Column Selection for Use in Protein Purification
Published on: September 21, 2011
How protein chemists learned about the hydrophobic factor
1Emeritus Faculty, Duke University Medical Center, Durham, North Carolina 27710, USA. candj@dial.pipex.com
Summary
The hydrophobic force, crucial for protein folding, was initially overlooked despite early proposals. Its significance in polypeptide chain folding was recognized decades later, impacting protein science.
Area of Science:
- Biochemistry
- Molecular Biology
- Physical Chemistry
Background:
- The hydrophobic force is widely accepted as the primary driver for polypeptide chain folding into globular structures.
- Early recognition of hydrophobicity's role in protein folding by Langmuir and Bernal in 1938 was overshadowed by the competing "cyclol hypothesis."
Observation:
- The hydrophobic principle gained prominence in protein science following a 1959 review by W. Kauzmann.
- A theoretical paper by Frank and Evans (1945) provided a conceptual framework for understanding the origins of hydrophobicity in water structure.
Findings:
- Hydrophobic interactions are now accepted as the primary energetic driver for the folding of polypeptide chains into compact globular proteins.
- The acceptance of hydrophobicity as a key factor in protein folding was significantly influenced by theoretical work on water structure.
Implications:
- Understanding hydrophobic forces is essential for deciphering protein structure and function.
- This principle underpins research in drug design, protein engineering, and understanding diseases related to protein misfolding.
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