Correlation between sequence hydrophobicity and surface-exposure pattern of database proteins

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Correlation between sequence hydrophobicity and surface-exposure pattern of database proteins.

Hydrophobicity is thought to be one of the primary forces driving the folding of proteins. On average, hydrophobic residues occur preferentially in the core, whereas polar residues tend to occur at the surface of a folded protein. By analyzing the known protein structures, we quantify the degree to which the hydrophobicity sequence of a protein correlates with its pattern of surface exposure. W...

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Some properties of compounds in degrading bacteria are required for biodegradation of contaminants to higher performance. Those strains which have a high percentage of these features are more effective at biodegradation. The present experiments were designed to measure these parameters. In this study, measurement of cell surface hydrophobic-degrading bacteria was designed which oil was separate...

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Hydrophobicity at the surface of proteins.

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relationship between cell surface hydrophobicity and degradation of hexadecane

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ژورنال

عنوان ژورنال: Protein Science

سال: 2004

ISSN: 0961-8368,1469-896X

DOI: 10.1110/ps.03431704