BLG 311 Lecture Notes - Lecture 4: Coiled Coil, Alpha Helix, Nuclear Membrane
24 May 2016
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Are organised into 6 groups (in humans); classes i to vi and (class v lamins) Undergo series or posttranslational modifications (mostly phosphorylation, not clearly defined, and removal of phosphate at the atp promotes assembly as opposed to being phosphorylated, removed by phosphatases) Like any protein structure, there is an amino terminus and carboxyl terminal. Two subunits (alpha helical monomer) interact with other subunits, in a parallel manner, to form a 48 nm dimer (the h bonds in the alpha structure prevents excessive stretching, stabilizing it) Coiled coil alpha helices twisting around each other; in this case there are two helices, and the hydrophobic regions come in contact. Two dimer in an anti-parallel (n and c to each other) direction form a staggered tetramer. Finally, 8 tetramers attach laterally and loosely. This loose association is an immature filament. Undergoes a step called compaction which promotes tighter association allowing for reduction of size, from 20 nm to 10 nm (tighter association).
