Use of molecular mechanics for secondary structure prediction. Is it possible to reveal α‐helix?

FEBS Letters

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