dorsal/arxiv
View SchemaCorrelation between sequence hydrophobicity and surface-exposure pattern of database proteins
| Authors | Susanne Moelbert, Eldon Emberly, Chao Tang |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0312010 |
| URL | https://arxiv.org/abs/q-bio/0312010 |
Abstract
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 tends 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. We have assessed the statistical significance of this correlation for several hydrophobicity scales in the literature, and find that the computed correlations are significant but far from optimal. We show that this less than optimal correlation arises primarily from the large degree of mutations that naturally occurring proteins can tolerate. Lesser effects are due in part to forces other than hydrophobicity and we quantify this by analyzing the surface exposure distributions of all amino acids. Lastly we show that our database findings are consistent with those found from an off-lattice hydrophobic-polar model of protein folding.
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"abstract": "Hydrophobicity is thought to be one of the primary forces driving the folding\nof proteins. On average, hydrophobic residues occur preferentially in the core,\nwhereas polar residues tends to occur at the surface of a folded protein. By\nanalyzing the known protein structures, we quantify the degree to which the\nhydrophobicity sequence of a protein correlates with its pattern of surface\nexposure. We have assessed the statistical significance of this correlation for\nseveral hydrophobicity scales in the literature, and find that the computed\ncorrelations are significant but far from optimal. We show that this less than\noptimal correlation arises primarily from the large degree of mutations that\nnaturally occurring proteins can tolerate. Lesser effects are due in part to\nforces other than hydrophobicity and we quantify this by analyzing the surface\nexposure distributions of all amino acids. Lastly we show that our database\nfindings are consistent with those found from an off-lattice hydrophobic-polar\nmodel of protein folding.",
"arxiv_id": "q-bio/0312010",
"authors": [
"Susanne Moelbert",
"Eldon Emberly",
"Chao Tang"
],
"categories": [
"q-bio.BM"
],
"title": "Correlation between sequence hydrophobicity and surface-exposure pattern of database proteins",
"url": "https://arxiv.org/abs/q-bio/0312010"
},
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