[Left-handed helix conformation of poly-L-proline II type in globular proteins. Statistics of incidence and a role of sequence]

P K Vlasov; G T Kilosanidze; D L Ukrainskiĭ; A V Kuz'min; V G Tumanian; N G Esipova

[Left-handed helix conformation of poly-L-proline II type in globular proteins. Statistics of incidence and a role of sequence]

Biofizika. 2001 May-Jun;46(3):573-6.

[Article in Russian]

Authors

P K Vlasov¹, G T Kilosanidze, D L Ukrainskiĭ, A V Kuz'min, V G Tumanian, N G Esipova

Affiliation

¹ Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, ul. Vavilova 32, Moscow, 119991 Russia.

PMID: 11449562

Abstract

Regions of left-handed polyproline II type conformation in globular proteins were studied throughout the PDB bank. The length and sequence of corresponding fragments were analyzed. It was found that a lot of tetrapeptides (from combinatorial possible ones) show the tendency to be included in the left-handed helices. Much more tetrapeptides do not occur in this structure type.

Publication types

English Abstract
Letter

MeSH terms

Amino Acid Sequence
Data Interpretation, Statistical
Databases, Factual
Molecular Sequence Data
Peptides / chemistry*
Protein Conformation
Proteins / chemistry*

Substances

Peptides
Proteins
polyproline