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Hydrophobicity regained
Author(s) -
Andrew Karplus P.
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560060618
Subject(s) - side chain , solvation , hydrogen bond , energetics , equating , chemistry , aqueous solution , polar , computational chemistry , amino acid , delta , chemical physics , thermodynamics , stereochemistry , solvent , organic chemistry , physics , molecule , mathematics , biochemistry , statistics , astronomy , rasch model , polymer
A widespread practice is to use free energies of transfer between organic solvents and water (Δ G transfer ° ) to define hydrophobicity scales for the amino acid side chains. A comparison of four Δ G transfer ° scales reveals that the values for hydrogen‐bonding side chains are highly dependent on the non‐aqueous environment. This property of polar side chains violates the assumptions underlying the paradigm of equating Δ G transfer ° with hydrophobicity or even with a generic solvation energy that is directly relevant to protein stability and ligand binding energetics. This simple regaining of the original concept of hydrophobicity reveals a flaw in approaches that use Δ G transfer ° values to derive generic estimates of the energetics of the burial of polar groups, and allows the introduction of a “pure” hydrophobicity scale for the amino acid residues.