Slow muscle fibres in athletes

Endurance athletes exercise for long periods of time;

Respire / release energy aerobically;
Or too much lactate would accumulate;
Slow twitch fibres adapted to aerobic metabolism;
As have many mitochondria;
Site of Krebs cycle;
And electron transport chain;
Much ATP formed;
Also are resistant to fatigue;
Short-distance athletes (fast muscle)
ref to fast twitch muscle fibres;
ref creatine phosphate / eq in these fibres;
ref to storage of ATP;
idea that energy obtained from ATP (from creatine phosphate);
idea that athlete would need to respire anaerobically;
ref to glycolysis producing atp rapidly;
idea that glycolysis occurs in the cytoplasm;
idea of some aerobic respiration because of oxygen present; description of
lactate fermentation:
(-Pyruvate obtained from glycolysis is reduced to lactate)
(-This regenerates NAD by oxidising the reduced NAD formed in glycolysis)
(-The NAD can then be re-used so glycolysis can continue and form ATP)

The contraction of muscle with its components 3.7.3

Function of Calcium ions
reference to {calcium ions / eq} released by sarcoplasmic reticulum ;
activate myosin / cause myosin to hydrolyse ATP ;
bind to / cause change in shape of troponin ;
cause tropomyosin to detach from actin filament / expose binding site (in actin) ;
Function of actin
reference to shape producing myosin binding sites ;
myosin globular heads fit / eq ;
Function of myosin
reference to globular heads (on the polypeptide chains) ;
reference to ATP on these heads ;
reference to phosphates ;
idea that head may be able to act as ATPase enzyme ; The hydrolysis of ATP to
ADP and Pi occurs due to the action of myosin itself. Therefore myosin has an in-

built enzymatic activity, it acts as an ATPase.

Troponin
attached to tropomyosin ;
ref to 3 sub units ;
ref to binding properties;
(one binds to actin, one to tropomyosin, one to calcium ions)
Tropomyosin
Long chain / eq ;
covers the myosin binding sites ;
on actin ;
Muscle contraction*
Calcium ions bind to troponin;
Remove blocking action of tropomyosin / exposes actin binding sites;
ATP allows myosin to join / bind to actin / form cross-bridge;
allows sliding of the actin & myosin filaments;
Re-cocks myosin cross bridge The bridge refers to the attachment of myosin to
actin. This must be broken in order for myosin to swing to its new position / allows
detachment from actin (due to binding of ATP);
Enables calcium ions to be pumped back in; Once calcium has done its job it
should be pumped back into the sarcoplasmic reticulum (against a concentration
gradient) so that further contractions of the muscle are inhibited.
hydrolysis of ATP releases energy / eq; This is how we get energy from ATP.
Hydrolyzed to ADP and Pi.
which changes configuration of myosin head / eq; Myosin is a protein hence
addition of ATP , hydrolysis of it or dissociasion of inorganic phosphate etc re-shapes
the bonds in3ary structure and hence myosin changes shape.
Phosphocreatine allows regeneration of ATP without respiration;
Phosphocreatine releases Pi to join ADP;
Sliding filament hypothesis
tropomyosin covers binding site on actin;
calcium ions remove tropomyosin;
myosin binding sites exposed on actin;
binding / calcium ions increase ATPase activity; Same as above.
breaks down ATP yielding energy; Same as above
used to re-cock myosin head;
ATP attachment cause actomyosin head to break /ATP required for separation of
actin and myosin/cross bridges;
#2
Myosin & actin filaments slide over one another;

 idea that sarcomere contracts;

ref to simultaneous contraction; (of what? Of all the myosin heads wrapped
around to form the thick filaments you see in sarcomeres. Check the photos in the
powerpoint presentation or your textbook.
idea that myofibrils / muscle fibres contract;
idea that sarcomere returns to original length at relaxation;
A-bands stay the same length, I-band gets shorter, H-zones get shorter (the zone
made up exclusively of myosin molecules/ thick filamentscheck the photos!) ,
sarcomere overall gets shorter (at contraction)
Also didn't understand..
CGP mark scheme
Acetyl coA (from link reaction) combines with oxaloacetate to form citrate
Coenzyme returns to link reaction for re-use
6C citrate converted to 5C
Decarboxylation and dehydrogenation occurs
Hydro used to produce NAD from FAD
5C molecule converted to 4C
Decarboxylation and dehydrogenation occur to produce 1 FAD and 2 NADH
ATP made when phosphate directly transferred to the constituent ADP (substratelevel phosphorylation) No need to worry about this term used here. You just need to
know the difference between substrate-level and oxidative phosphorylation.
The citrate is then converted to oxaloacetate (regeneration of 6C from 4C)
Link reaction We called it pyruvate processing. The transfer of pyruvate into the
mitochondrial matrix and its conversion to acetyl CoA.
pyruvate {decarboxylated / eq} ;
hydrogen joins (from pyruvate) to NAD to reduce it ;
pyruvate acetate ;
acetate {combines / joins with / eq} coenzyme A;
ref to formation of acetyl coenzyme A;
ref to products (two acetyl coenzyme A, two CO2 molecules, two reduced NAD);
no ATP made ;
Your notes are somewhat extremely detailed...I wouldn't worry that much if I were
you.