[Left-handed helix conformation of poly-L-proline II type in globular proteins. Statistics of incidence and a role of sequence].
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.
Vlasov
P K
PK
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, ul. Vavilova 32, Moscow, 119991 Russia.
Kilosanidze
G T
GT
Ukrainskiĭ
D L
DL
Kuz'min
A V
AV
Tumanian
V G
VG
Esipova
N G
NG
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*
D010455:Peptides; D011506:Proteins; C011083:polyproline