On hydrophobicity correlations in protein chains

A Irbäck; E Sandelin

doi:10.1016/S0006-3495(00)76472-1

On hydrophobicity correlations in protein chains

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	2252-8
Number of pages	7
Journal	Biophysical Journal
Volume	79
Issue number	5
DOIs	https://doi.org/10.1016/S0006-3495(00)76472-1
Publication status	Published - 2000 Nov

Free keywords

Biophysical Phenomena
Biophysics
Enzymes
Models, Chemical
Protein Folding
Proteins

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10.1016/S0006-3495(00)76472-1

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title = "On hydrophobicity correlations in protein chains",

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.",

keywords = "Biophysical Phenomena, Biophysics, Enzymes, Models, Chemical, Protein Folding, Proteins",

author = "A Irb{\"a}ck and E Sandelin",

year = "2000",

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AU - Irbäck, A

AU - Sandelin, E

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AB - 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.

KW - Biophysical Phenomena

KW - Biophysics

KW - Enzymes

KW - Models, Chemical

KW - Protein Folding

KW - Proteins

U2 - 10.1016/S0006-3495(00)76472-1

DO - 10.1016/S0006-3495(00)76472-1

M3 - Article

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SN - 0006-3495

VL - 79

SP - 2252

EP - 2258

JO - Biophysical Journal

JF - Biophysical Journal

IS - 5

ER -

On hydrophobicity correlations in protein chains

Abstract

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