On Hydrophobicity Correlations in Protein Chains
نویسندگان
چکیده
منابع مشابه
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...
متن کاملOn Hydrophobicity Correlations in Protein Chains Submitted to Biophysical Journal
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 signiicant 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 ...
متن کاملEvidence for nonrandom hydrophobicity structures in protein chains.
The question of whether proteins originate from random sequences of amino acids is addressed. A statistical analysis is performed in terms of blocked and random walk values formed by binary hydrophobic assignments of the amino acids along the protein chains. Theoretical expectations of these variables from random distributions of hydrophobicities are compared with those obtained from functional...
متن کاملHydrophobicity Patterns in Protein Folding
Key words Classification system and/or index terms (if any) Supplementary bibliographical information Language ISSN and key title ISBN Recipient's notes Number of pages Price Security classification Distribution by (name and address) I, the undersigned, being the copyright owner of the abstract of the above-mentioned dissertation, hereby grant to all reference sources the permission to publish ...
متن کاملSite-directed analysis on protein hydrophobicity
Hydrophobicity of a protein is considered to be one of the major intrinsic factors dictating the protein aggregation propensity. Understanding how protein hydrophobicity is determined is, therefore, of central importance in preventing protein aggregation diseases and in the biotechnological production of human therapeutics. Traditionally, protein hydrophobicity is estimated based on hydrophobic...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2000
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(00)76472-1