Identification of amino acid sequences with good folding properties in an off-lattice model
(1997) In Physical Review E 55(1 SUPPL. B). p.860-867- Abstract
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... (More)
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.
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- author
- Irbäck, Anders LU ; Peterson, Carsten LU and Potthast, Frank LU
- organization
- publishing date
- 1997-01
- type
- Contribution to journal
- publication status
- published
- in
- Physical Review E
- volume
- 55
- issue
- 1 SUPPL. B
- pages
- 8 pages
- publisher
- American Physical Society
- external identifiers
-
- scopus:18844424885
- ISSN
- 1063-651X
- DOI
- 10.1103/PhysRevE.55.860
- language
- English
- LU publication?
- yes
- id
- 934e7dc7-0ba3-4c49-991f-900f8ad21a65
- date added to LUP
- 2016-08-17 17:58:14
- date last changed
- 2024-01-04 10:59:37
@article{934e7dc7-0ba3-4c49-991f-900f8ad21a65, abstract = {{<p>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.</p>}}, author = {{Irbäck, Anders and Peterson, Carsten and Potthast, Frank}}, issn = {{1063-651X}}, language = {{eng}}, number = {{1 SUPPL. B}}, pages = {{860--867}}, publisher = {{American Physical Society}}, series = {{Physical Review E}}, title = {{Identification of amino acid sequences with good folding properties in an off-lattice model}}, url = {{http://dx.doi.org/10.1103/PhysRevE.55.860}}, doi = {{10.1103/PhysRevE.55.860}}, volume = {{55}}, year = {{1997}}, }