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Hydrophobicity scale for proteins based on inverse temperature transitions
D W Urry1, D C Gowda, T M Parker
1Laboratory of Molecular Biophysics, School of Medicine, University of Alabama, Birmingham 35294-0019.
Biopolymers
|September 1, 1992
Summary
Scientists developed a new hydrophobicity scale for amino acids based on transition temperature (Tt). This scale enables controlling protein folding at body temperature, potentially driving isothermal free energy transduction.
Area of Science:
- Biochemistry
- Protein Folding
- Thermodynamics
Background:
- Proteins typically fold with hydrophobic residues shielded from water.
- Reversible protein folding driven by hydrophobic interactions often occurs via inverse temperature transitions, where folding increases with temperature.
- In warm-blooded animals, the transition temperature (Tt) dictates the folded state of polypeptides at body temperature.
Purpose of the Study:
- To introduce a novel hydrophobicity scale for amino acids.
- To establish a method for controlling protein folding at physiological temperatures.
Main Methods:
- A new hydrophobicity scale was developed using Tt values of amino acid residues.
- Amino acids were incorporated as guests within a natural repeating peptide sequence.
- High polymers of this sequence exhibited reversible inverse temperature transitions.
Main Results:
- A new hydrophobicity scale based on Tt was successfully established.
- Methods were demonstrated to alter Tt, enabling folding below physiological temperatures.
- This allows for isothermal and reversible induction of hydrophobic folding.
Conclusions:
- Controlling Tt is a viable mechanism for inducing hydrophobic folding.
- This control offers a pathway for proteins to perform isothermal free energy transduction.