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Cytoskeleton protein
Uni of Notts, Structure, function, & analysis of Proteins, year 2, topics 12-13
| Term | Definition |
|---|---|
| Why the +end of actin grows faster | + end requires lower critical profilin concentration (binds preferentially to ATP-actin over ADP-actin), so ATP-actin monomers add more easily there |
| Bacterial locomotion using actin | Bacterial proteins like ActA recruit ARP2/3 to polymerise actin & propel the bacterium |
| Phalloidin (deathcap) mode of action | Stabilises F-actin excessively, blocking normal actin dynamics & intracellular transport |
| Pericentriolar material | Protein-rich matrix around centrioles that nucleates & anchors microtubules. Each arranged perpendicularly |
| Microtubule assymetry | Tubulin dimers bind head-to-tail & only β-tubulin contains the exchangeable GTP site |
| Dynamic instability importance in mitosis | Rapid growth/rescue & shrinkage/catastrophe allow spindle microtubules to search for & move chromosomes during anaphase |
| γ-TuRC complex | Nucleates new microtubules by templating tubulin assembly |
| Catastrophe factors | Proteins that destabilise microtubule dimer ends into ram's horns & promote depolymerisation. Can be controlled to prevent anaphase |
| Specific stability of intermediate filaments | Their assembly is nucleotide-independent & forms highly insoluble rope-like structures |
| Intermediate filament regulation | Post-translational modifications such as phosphorylation rather than nucleotide binding |
| Myosin contraction | Myosin II heads pull actin filaments past one another using ATP-driven power strokes. Often contain regulatory domains like calmodulin |
| Changes in mysin-acting binding affinity after contraction | ATP binding lowers myosin affinity for actin, allowing detachment before the next stroke |
| Actomyosin in cytokinesis | Actin & myosin II form a contractile ring that contracts to pinche the cell into two daughter cells |
| Special traits of myosin VI | Unlike most myosins, it moves toward the minus end of actin filaments rather than the + |
| Processive motor protein | A motor that takes multiple sequential steps without detaching from its filament (e.g., myosin V) |
| Kinesin & dynein directionality | Kinesin usually moves to the + end; dynein usually moves to the − end |
| kinesins 8 nm step movements | Each step corresponds to the length of one αβ-tubulin heterodimer |
| Kinesin directionality determination | Neck linker region controls stepping orientation rather than the motor head itself |
| Cilia & flagella generated movement | Dynein-driven sliding between adjacent microtubule bundles produces bending & resetting allowing for propulsion |
| glycine abundance in collagen | Its tiny side chain reduce steric hinderance allowing tight packing in the collagen triple helix core by lining the inside |
| Hydroxyproline (Hpr) in collagen | Hydroxyproline stabilises the triple helix through hydrogen bonding |
| Age related collagen inflexibility | Continued lysine-derived crosslinking never stops then accumulates & stiffens collagen fibres |
| How spider silk is both strong & flexible | β-sheet crystalline regions provide strength while glycine-rich regions allow flexibility |
| Spidroin fibre formation *example* | Ion exchange, dehydration, shear force, & pH changes convert soluble proteins into fibres |
| F-actin formation & structure | Doesn't require cofactors (e.g., thymosine) to form but can be affected by them. Double helix with 14 G-actin per turn |
Created by:
Denny12
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