Ab initio tertiary-fold prediction of helical and non-helical protein chains using a genetic algorithm
In this study, protein structures were predicted using a genetic algorithm. Optimal structures were selected according to basic protein-building principles. Having previously applied this approach to proteins with helical topology, this paper reports preliminary results on 3 proteins with mixed topo...
Gespeichert in:
| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
February 1996
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| In: |
International journal of biological macromolecules
Year: 1996, Jahrgang: 18, Heft: 1, Pages: 1-4 |
| ISSN: | 1879-0003 |
| DOI: | 10.1016/0141-8130(95)01036-X |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/0141-8130(95)01036-X Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/014181309501036X 
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| Verfasserangaben: | T. Dandekar, P. Argos |
MARC
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| 520 | |a In this study, protein structures were predicted using a genetic algorithm. Optimal structures were selected according to basic protein-building principles. Having previously applied this approach to proteins with helical topology, this paper reports preliminary results on 3 proteins with mixed topology (helical and non-helical, e.g. sheet). The method seems to be generally applicable to protein-fold prediction since topology predictions close to the observed experimental structures are obtained. | ||
| 650 | 4 | |a Main-chain topology | |
| 650 | 4 | |a Protein structure prediction | |
| 650 | 4 | |a Simulated evolution | |
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