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Anders Irbäck. Photo.

Anders Irbäck

Professor

Anders Irbäck. Photo.

Identification of amino acid sequences with good folding properties in an off-lattice model

Author

  • Anders Irbäck
  • Carsten Peterson
  • Frank Potthast

Summary, in English

Folding properties of a two-dimensional toy protein model containing only two amino acid types, hydrophobic and hydrophilic, respectively, are analyzed. An efficient Monte Carlo procedure is employed to ensure that the ground states are found. The thermodynamic properties are found to be strongly sequence dependent in contrast to the kinetic ones. Hence, criteria for good folders are defined entirely in terms of thermodynamic fluctuations. With these criteria sequence patterns that fold well are isolated. For 300 chains with 20 randomly chosen binary residues approximately 10% meet these criteria. Also, an analysis is performed by means of statistical and artificial neural network methods from which it is concluded that the folding properties can be predicted to a certain degree given the binary numbers characterizing the sequences.

Department/s

  • Computational Biology and Biological Physics

Publishing year

1997-01

Language

English

Pages

860-867

Publication/Series

Physical Review E

Volume

55

Issue

1 SUPPL. B

Document type

Journal article

Publisher

American Physical Society

Status

Published

ISBN/ISSN/Other

  • ISSN: 1063-651X