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13 Cards in this Set

  • Front
  • Back
runs from z line to m line

connects z line to thick filaments, stabalizes
each thing filament has one nebulin molec, anchors capping protein and helps set length
actin capping protein of thin filaments, protects em from depolymerization
Cap Z
cap at the Z line en, helps anchor thin filament
myosin molecule
thick filament dimer, tail(light myosin), hinge (S2) and business end (s1)(heavy myosin)
what special structures does the head region contain
an ATPAse and an actin binding domain
what governs the rate of ATPase activity and therefore the speed of muscle shortening??
isozymes of myosin only
tropomyosin (not tropomodulin)
winds around the actin helix , covers the actin binding sites
a globular protein bound to tropomyosin
has three sites
TnI - inhibitory, inhibits activation of myosin ATPase by actin
TnT - site of attachment of troponin to tropomyosin
TnC - binds Ca

Ca binds to troponin C, causing changes in regulatory proteins that then shift tropomyosin out of the way
isotonic vs isometric contraction
isotonic - filaments slide

isometric - minimal sliding but force is produced
length of muscle - number of sites of interaction between thin and thick filaments

amount of force that can be developed, potential force
optimal overlap
have a range of optimal ovelap, due to bare zone in thick filaments where there are no heads so can't make anymore connections and before the thin filaments start to overlap
Regulation of striated muscle, is it on or off usually?
A disinhibition system

striated muscle is always ON, but the troponin/tropomyosin system inhibits it

Ca comes along and moves the troponin-->tropomyosin causing DISINHIBITION