On hydrophobicity correlations in protein chains

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Abstract

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.

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Keywords

  • Biophysical Phenomena, Biophysics, Enzymes, Models, Chemical, Protein Folding, Proteins
Original languageEnglish
Pages (from-to)2252-8
Number of pages7
JournalBiophysical Journal
Volume79
Issue number5
Publication statusPublished - 2000 Nov
Publication categoryResearch
Peer-reviewedYes