Structure of coiled beta-beta-hairpins and beta-beta-corners.
Two types of super-secondary structure, coiled beta-beta-hairpins and beta-beta-corners, are considered in this paper. A beta-beta-corner can be represented as a long beta-beta-hairpin folded orthogonally on itself so that the strands, when passing from one layer to the other, rotate in a right-handed direction about an imaginary axis. It is shown that a beta-beta-hairpin, forming a coiled coil structure or a beta-beta-corner, is right-handed when viewed from the concave side. These unique arrangements of beta-strands in the coiled beta-beta-hairpins and beta-beta-corners are of particular value in protein modelling and prediction.
Efimov
A V
AV
Institute of Protein Research, Academy of Sciences of the USSR, Pushchino, Moscow Region.
D000426:Alcohol Dehydrogenase / Q000737:chemistry; D010450:Endopeptidases / Q000737:chemistry; D007375:Interleukin-1 / Q000737:chemistry; D007770:L-Lactate Dehydrogenase / Q000737:chemistry; D011487:Protein Conformation; D012260:Ribonucleases / Q000737:chemistry; D014361:Trypsin Inhibitors / Q000737:chemistry
D007375:Interleukin-1; D014361:Trypsin Inhibitors; D000426:Alcohol Dehydrogenase; D007770:L-Lactate Dehydrogenase; D012260:Ribonucleases; D010450:Endopeptidases