Hydrophobicity of amino acid residues in globular proteins.

@article{Rose1985HydrophobicityOA,
  title={Hydrophobicity of amino acid residues in globular proteins.},
  author={George D. Rose and A R Geselowitz and G J Lesser and R H Lee and Micheal H. Zehfus},
  journal={Science},
  year={1985},
  volume={229 4716},
  pages={
          834-8
        }
}
During biosynthesis, a globular protein folds into a tight particle with an interior core that is shielded from the surrounding solvent. The hydrophobic effect is thought to play a key role in mediating this process: nonpolar residues expelled from water engender a molecular interior where they can be buried. Paradoxically, results of earlier quantitative analyses have suggested that the tendency for nonpolar residues to be buried within proteins is weak. However, such analyses merely classify… 
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    J. Chem. Inf. Comput. Sci.
  • 2001
Hydrophobicity is a useful concept to rationalize the role played by amino acid residues in terms of buried or exposed conformation with regard to the aqueous environment in proteins. The
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The hydrophobic variation of amino acid residues at various ranges in membrane and aqueous parts of membrane proteins is analysed to understand their structure and stability.
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This paper experimentally shows that the hydrophobic residues collectively reveal different composition patterns over different secondary structure elements, and quantitatively compares them using the statistical moments.
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The ability to predict surface accessibility of hydrophobic residues directly from the sequence is of great help in choosing the sites of chemical modification or specific mutations and in the studies of protein stability and molecular interactions.
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The study of protein stability is currently undergoing a dramatic change. Early work, especially after Kauzmann (1959), centered on the analysis of simple chemical model systems to determine the
Prediction of transmembrane helices from hydrophobic characteristics of proteins.
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A surrounding hydrophobicity scale applicable to membrane proteins is developed and a predictive scheme based on this scale predicts from amino acid sequence, transmembrane segments in PRC and randomly selected 26 membrane proteins to 80% level of accuracy.
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