Hydrophobicity scale for proteins based on inverse temperature transitions

Authors

  • Dan W. Urry,

    Corresponding author
    1. Laboratory of Molecular Biophysics, School of Medicine, The University of Alabama in Birmingham, Post Office Box 300, University Station, Birmingham, Alabama 35294-0019
    • Laboratory of Molecular Biophysics, School of Medicine, The University of Alabama in Birmingham, Post Office Box 300, University Station, Birmingham, Alabama 35294-0019
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  • D. Channe Gowda,

    1. Laboratory of Molecular Biophysics, School of Medicine, The University of Alabama in Birmingham, Post Office Box 300, University Station, Birmingham, Alabama 35294-0019
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  • Timothy M. Parker,

    1. Laboratory of Molecular Biophysics, School of Medicine, The University of Alabama in Birmingham, Post Office Box 300, University Station, Birmingham, Alabama 35294-0019
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  • Chi-Hao Luan,

    1. Laboratory of Molecular Biophysics, School of Medicine, The University of Alabama in Birmingham, Post Office Box 300, University Station, Birmingham, Alabama 35294-0019
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  • Michael C. Reid,

    1. Laboratory of Molecular Biophysics, School of Medicine, The University of Alabama in Birmingham, Post Office Box 300, University Station, Birmingham, Alabama 35294-0019
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  • Cynthia M. Harris,

    1. Laboratory of Molecular Biophysics, School of Medicine, The University of Alabama in Birmingham, Post Office Box 300, University Station, Birmingham, Alabama 35294-0019
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  • Asima Pattanaik,

    1. Laboratory of Molecular Biophysics, School of Medicine, The University of Alabama in Birmingham, Post Office Box 300, University Station, Birmingham, Alabama 35294-0019
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  • R. Dean Harris

    1. Laboratory of Molecular Biophysics, School of Medicine, The University of Alabama in Birmingham, Post Office Box 300, University Station, Birmingham, Alabama 35294-0019
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Abstract

In general, proteins fold with hydrophobia residues buried, away from water. Reversible protein folding due to hydrophobia interactions results from inverse temperature transitions where folding occurs on raising the temperature. Because homoiothermic animals constitute an infinite heat reservoir, it is the transition temperature, Tt, not the endothermic heat of the transition, that determines the hydrophobically folded state of polypeptides at body temperature. Reported here is a new hydrophobicity scale based on the values of Tt for each amino acid residue as a guest in a natural repeating peptide sequence, the high polymers of which exhibit reversible inverse temperature transitions. Significantly, a number of ways have been demonstrated for changing Tt such that reversibly lowering Tt, from above to below physiological temperature becomes a means of isothermally and reversibly driving hydrophobic folding. Accordingly, controlling Tt, becomes a mechanism whereby proteins can be induced to carry out isothermal free energy transduction. © 1992 John Wiley & Sons, Inc.

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