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 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.
Dandekar
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T
European Molecular Biology Laboratory, Heidelberg, Germany.
Argos
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P
D000465:Algorithms; D000595:Amino Acid Sequence; D006860:Hydrogen Bonding; D008957:Models, Genetic; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics
C029152:G-substrate; D009419:Nerve Tissue Proteins; D010940:Plant Proteins; D011506:Proteins; C024934:crambin protein, Crambe abyssinica