Hydrophobicity scales are values that define the relative hydrophobicity or hydrophilicity of amino acid residues. The more positive the value, the more hydrophobic are the amino acids located in that region of the protein. These scales are commonly used to predict the transmembrane alpha-helices of membrane proteins. When consecutively measuring amino acids of a protein, changes in value indicate attraction of specific protein regions towards the hydrophobic region inside lipid bilayer.
The hydrophobic or hydrophilic character of a compound or amino acid is its hydropathic character,[1] hydropathicity, or hydropathy.
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Hydrophobicityscales are values that define the relative hydrophobicity or hydrophilicity of amino acid residues. The more positive the value, the more...
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the basis of hydrophobicityscales. Because the interior of the bilayer and the interiors of most proteins of known structure are hydrophobic, it is presumed...
but also hydrophobic), those of which were much greater than that of known polar amino acids such as serine and threonine. Hydrophobicityscales, which...
residue-level models, the stickiness parameters have been derived from hydrophobicityscales or from a bioinformatic analysis of crystal structures of folded...
separation of transmembrane proteins with a higher hydrophobic thickness into the lipid rafts. Hydrophobicityscales Cell membrane Lipid raft Duque, D.; Li, X...
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membrane-spanning regions contain more hydrophobic residues than other parts of the protein, however applying different hydrophobicscales altered the prediction results...
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the number of known membrane protein stabilities. She created a hydrophobicityscale to describe protein side-chains. Fleming performed some of the first...
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cost and difficulty of predicting protein structure, using only the hydrophobicity of the amino acids in the protein to predict the protein structure....
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properties, e.g., enhanced[clarification needed] stability, volatility, and hydrophobicity. Several fluorocarbons and their derivatives are commercial polymers...
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