A tetrapeptide‐based method for polyproline II‐type secondary structure prediction

Proteins: Structure, Function and Bioinformatics - Tập 61 Số 4 - Trang 763-768 - 2005
Peter K. Vlasov1, Anna Vlasova, V. G. Tumanyan, Esipova Ng
1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia. [email protected]

Tóm tắt

AbstractWe describe a new method for polyproline II‐type (PPII) secondary structure prediction based on tetrapeptide conformation properties using data obtained from all globular proteins in the Protein Data Bank (PDB). This is the first method for PPII prediction with a relatively high level of accuracy (∼60%). Our method uses only frequencies of different conformations among oligopeptides without any additional parameters. We also attempted to predict α‐helices and β‐strands using the same approach. We find that the application of our method reveals interrelation between sequence and structure even for very short oligopeptides (tetrapeptides). Proteins 2005. © 2005 Wiley‐Liss, Inc.

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Tài liệu tham khảo

10.1006/jmbi.2000.3981

10.1093/emboj/19.20.5324

10.4049/jimmunol.167.1.578

10.1002/bip.360370406

10.1021/bi0023605

10.1080/07391102.1996.10508117

10.1016/S0167-4838(99)00209-5

10.1038/nsb1101-998

10.1016/0006-291X(87)90736-4

10.1006/jmbi.1993.1047

10.1002/pro.5560031223

10.1016/S0010-4825(01)00013-0

10.1021/bi00199a028

10.1110/ps.8.3.587

10.1073/pnas.71.10.4217

10.1093/proeng/gzg019

Vlasov PK, 2001, Left‐handed conformation of poly‐L‐proline II type in globular proteins, Biophysics, 46, 546

10.1002/(SICI)1097-0134(19990515)35:3<313::AID-PROT5>3.0.CO;2-1

10.1038/5794

Ramensky VE, 2000, How do point amino acid substitution affect the protein structure?, Biophysics, 45, 215

10.1002/(SICI)1097-0134(19980215)30:3<228::AID-PROT2>3.0.CO;2-G

10.1023/A:1026366706677