On hydrophobicity correlations in protein chains.
We study the statistical properties of hydrophobic/polar model sequences with unique native states on the square lattice. It is shown that this ensemble of sequences differs from random sequences in significant ways in terms of both the distribution of hydrophobicity along the chains and total hydrophobicity. Whenever statistically feasible, the analogous calculations are performed for a set of real enzymes, too.
Irbäck
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A
Complex Systems Division, Department of Theoretical Physics, Lund University, Sölvegatan 14A, S-223 62 Lund, Sweden. irback@thep.lu.se
Sandelin
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E
D055592:Biophysical Phenomena; D001703:Biophysics; D004798:Enzymes / Q000737:chemistry; D008956:Models, Chemical; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D004798:Enzymes; D011506:Proteins