The amino terminal regions of proBNP and proANP oligomerize through leucine zipper-like coiled-coil motifs.
Structural assignment (a) Experimental 2[degrees] 3[degrees] technique structure structure SE-HPLC NA (b) Extended, nonglobular Sedimentation equilibrium ultracentrifugation NA NA CD Random coil, no helix NA Structural assignment (a) Experimental 4[degrees] Coiled-coil technique structure SE-HPLC NA NA Sedimentation equilibrium ultracentrifugation Monomer, not trimer No CD NA No (a) 2[degrees] structure refers to helix, [beta]-sheet, or random coil content; 3[degrees] structure refers to the overall three-dimensional shape of the molecule; and 4[degrees] structure refers to the putative state of association of individual molecules.
Synthesis of a model protein of defined secondary and quaternary structure: effect of chain length on the stabilization and formation of two-stranded [alpha]-helical coiled-coils.
A high score means that a particular amino acid is likely to be in a coiled-coil structure.
These can identify coiled-coil motifs in the proteins that viruses secrete and enable them to enter cells.