title: [Left-handed helix conformation of poly-L-proline II type in globular proteins. Statistics of incidence and a role of sequence].
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.
authors.affiliation: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, ul. Vavilova 32, Moscow, 119991 Russia.
authors.forename: P K
authors.initials: PK
authors.lastname: Vlasov
authors.forename: G T
authors.initials: GT
authors.lastname: Kilosanidze
authors.forename: D L
authors.initials: DL
authors.lastname: Ukrainskiĭ
authors.forename: A V
authors.initials: AV
authors.lastname: Kuz'min
authors.forename: V G
authors.initials: VG
authors.lastname: Tumanian
authors.forename: N G
authors.initials: NG
authors.lastname: Esipova
mesh_terms: D000595:Amino Acid Sequence; D003627:Data Interpretation, Statistical; D016208:Databases, Factual; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D010455:Peptides; D011506:Proteins; C011083:polyproline