FEBS Letters | |
Use of molecular mechanics for secondary structure prediction. Is it possible to reveal α‐helix? | |
Kutsenko, Alexey S1  Esipova, Natalia G2  Kilosanidze, Gelena T2  Tumanyan, Vladimir G2  | |
[1] Centre for Genomics and Bioinformatics, Karolinska Institute, P.O. Box 280, S-171 77 Stockholm, Sweden;Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia | |
关键词: Protein secondary structure; Structure prediction; α-Helix; Molecular mechanics; | |
DOI : 10.1016/S0014-5793(01)03212-4 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
A new approach to predicting protein standard conformations is suggested. The idea consists in modeling by molecular mechanics tools a continuous α-helical conformation for the whole protein. The profile of energy along the model α-helix reveals minima corresponding to real α-helical segments in the native protein. The 3/10-helices and β-turns including a local α-helical conformation may be detected as well. All α-helical segments in the test sample are delineated; mean residue by residue accuracy Q 3α is 79%. This non-statistical approach can shed light on the physical grounds of α-helix formation.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020311317ZK.pdf | 213KB | download |