week 3: 10.3 continued Flashcards
A band
regions of overlapping thick (myosin) and thin (actin) filaments
contains three sub divisions
three sub divisions of the A band
M line
H band
zone of overlap
M line
-centre of the A band
-proteins of the M line connect the central portion of each thick filament to neighboring thick filaments
-these dark-staining proteins help stabilise the positions of the thick filaments
H band
-lighter region on either side of the M line
- thick filaments only
zone of overlap
dark region where thin filaments are located between thick filaments
- three thick filaments surround each thin filament
- six thin filaments surround each thick filament
T tubules and sarcomere arrangement
T tubules encircle each sarcomere
where are the triads containing the T tubules located
zones of overlap, at the edges of the A band
significance of triad location
calcium ions released by the SR enter region where thick and thin filaments can interact
I band
region of the sarcomere that contains thin filaments
what does the I band extend from
A band of one sarcomere to A band of next
Z line and I band interaction
Z line bisects I band and marks boundaries between adjacent sarcomeres
Z line consists of
actinins proteins
interconnect thin filaments of adjacent sarcomeres
titin
extends from tips of thick filaments to attachment sights at Z line
function of titin
-helps to keep thick and thin filaments in proper alignment and aids in restoring resting sarcomere length after contraction
-helps muscle fiber resist extreme stretching that would disrupt contraction mechanism
thin filaments molecular structure
5-6 nm diamneter
1μm long
contains 4 main proteins: F-actin, nebulin, tropomyosin, troponin
Filamentous actin
twisted strand composed of two rows of 300-400 individual globular molecules of G actin
nebulin
-nebulin holds the F-actin strand together
-long strand of nebulin extends along F-actin strand in the cleft between the rows of G-actin molecules
what does each G-actin molecule contain
active sight where mysoin can bind
binding sight on G-actin in resting state
-troponin-tropomyosin complex prevents myosin binding
- strands of tropomyosin cover active sights on G-actin preventing actin-mysosin interaction
tropomyosin
double stranded protein that covers 7 active sights
bounded to one molecule of troponin midway along its length
troponin
3 globular subunits
how are troponin and tropomyosin locked into a complex
one globular subunit of troponin binds to tropomyosin locking them together as a complex
how is the troponin- tropomyosin complex locked into position
troponins second globular subunit binds to G actin holding complex into position
third subunit of troponin
has a receptor that binds to 2 Ca2+ ions
third troponin subunit in resting muscle
Ca2+ conc very low, binding sight is empty
when can a contraction occur
when the troponin-tropomyosin complex changes position,
exposing active sight on actin
when is the active sight on actin exposed
when calcium ions bind to receptors of troponin molecules
thick filaments
10-12nm diameter
1.6 μm long
mysoin arrangment in thick filament
contains approx 300 myosin molecules, each molecule made up of a pair of myosin subunits twisted around one another
long tail of myosin bound to
other myosin molecules in the thick filament
free head of myosin molecule
projects outwards to the nearest thin filament
two globular subunits
how are myosin molecules arranged
tails pointing towards the M line
no myosin heads in H region
elsewhere on filament, myosin heads arranged in spiral each facing one of the surrounding thin filaments
changes in sarcomere during contraction
A band stays the same width
Z lines move closer together
I band gets smaller
when the ends of a myofibril are free to move,
sarcomeres shorten simultaneously and the ends of the myofibril are pulled towards its centre
when one end of a myofibril is in a fixed position
the free (the insertion) end is pulled towards the fixed end (the origin)
what causes bone movement
muscle fibre contracts, pulls on tendons collagen fibers which are embedded in the bone,