9-11 Flashcards
What are Dynein and Kinesin?
The proteins that move along the microtubules
- dynein is a dimer and moves towards the negative end of the microtubules—> towards the centrosome (nucleus) - in 9+2 stucture moves along neighbouring doublet of microtubule dragging the other to cause bending
- Kinesin moves away from centrosome
Structure of microtubule
25nm across and made of α and β tubulin
Examples of movement mechanisms
x 7
- Outer hair cell motor
- Invertebrate photoreceptors
- ATP synthase
- RNA polymerase
- Flagella/cilia
- Actin/tubulin axonal transport
- Myosin/actin
Difference between parallel and series muscle unit structure
PARALLEL - each contract and force but then this is additive for each unit pulling so big force if parallel
SERIES - Adding contractile elements in series amplifies degree of movement as each segment shortens
Structure of muscle -
Myofibrils are bundles of protein filaments and then a group of myofibrils makes a muscle fibre (one single muscle cell) and then a bundle of fibres is a fascicle (sheathed in connective tissue) and then the whole skeletal muscle is multiple fascicles
What are the dark and light bands of striated (skeletal) muscle
Dark = A band = ANISOTROPIC
Light = I band = ISOTROPIC
Structure of a sarcomere
- single contractile unit of a muscle cell
- Z to Z line is 2 μm
- middle is m line which is the middle of the H zone, in the middle of the A band
- next to A band is I band and the Z line is in the middle of this
Structure of myosin
6 polypeptide chains
- Main is two supercoiled α helices so dimer with 2 heads and then three of these dimers per section
- the heads have the stiff neck with flexible hinge (each head has a ATP binding site)
- cocked state is the high energy state
- heads at 120 degrees and repeat every 43 nm
Structure of actin - F actin
G actin dimers into filaments
- polarised with + and - ends
- Tropomodulin at negative end
- g dimers to + at 5-10 x faster than loss at -
- 40nm sections and differ from 43 of heads of myosin - maybe purposeful desynchronisation (dont actually know why)
Other proteins of the thin actin filament
Tmod = tropomodulin at negative end
- Tropomyosin - cover myosin binding sites - is a dimer
- Troponin holds tropomyosin in place as its association is weak - moves it out of the way
- nebulin but do not know of function
Troponin structure
2 subunits
TnI inhibitory element and binds to actin
TnT binds to tropomyosin
TnC binds to Ca2+ and this causes the troponin to make a lateral shift of tropomyosin
What is titin?
largest protein in genome
- like a spring and maybe to protect against overstretching of sarcomere
- half life of roughly 3 days so continuously repaired
Structure of sarcomere diagram (so can draw)
diagram
- twice as many thin filaments as thick
What visually changes to sarcomere during contraction?
I band shrinks but the A band is constant size
- H zone reduces as well
What is the cross-bridge cycle?
x 6
- ATP binds to myosin heads and so dissociates from actin
- Break to ADP and Pi which causes head to cock into high energy position
- head attaches to myosin site on actin and releases Pi (strengthens binding and activates power stroke)
- Power stroke
- ADP dissociates from myosin head
- ATP attaches to head to cause dissociation from actin
What causes the start of contraction?
Release of Ca2+ from sarcoplasmic reticulum
- binds to TnC which moves tropomyosin
- force production rises rapidly for only a small rise in Ca2+
How do muscle fibres ensure Ca2+ gets to all sarcomeres?
invaginating membrane as otherwise diffusion would take too long
- so near synchronous activation
- done via t-tubules
Structure and purpose of t -tubules
90nm across and penetrate into fibre
- cause the shallow slope after depolarisation
- small and few ions
has Cl- ions to aid in repolarisation
- is K+ accumulates during intense activity can cause problems-volume
What is myotonia congenita
inherited condition which skeletal muscle goes into contracture
- chloride channel mutation of t-tubules