The formation of a paracrystalline structure from muscle F-actin and oligolysine.
At very low ionic strength (gamma less than 0.05) oligohomopolymers of lysine cause lateral association of muscle F-actin filaments into ordered structures which appear at low magnification in electron-micrographs as rigid needles. At higher magnification these aggregates display regular quasicrystalline patterns. The structures dissolve reversibly when the ionic strength is raised suggesting that F-actin filaments are crosslinked by oligolysine due to electrostatic forces.
Zechel
K
K
Max-Planck-Institut für Biophysikalische Chemie, Göttingen.
D000199:Actins / Q000378:metabolism* / Q000648:ultrastructure; D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D004560:Electricity; D008239:Lysine / Q000378:metabolism*; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009132:Muscles / Q000378:metabolism*; D009994:Osmolar Concentration; D011108:Polymers; D011817:Rabbits
D000199:Actins; D011108:Polymers; D008239:Lysine