ENERGY FOR

MUSCLE
CONTRACTION
Prasetyastuti
Dept. Of Biochemistry

- Muscle is the major biochemical transducer

(machine) that converts
potential (chemical) energy into
kinetic(mechanical) energy.
- Muscle, the largest single tissue in the human
body, makes up somewhat
-> less than 25% of body mass at birth,
-> more than 40% in the young adult,
-> and less than 30% in the aged adult.

Types of muscle found in vertebrates:

1. Skeletal : voluntary : Striated
2. cardiac : involuntary: Striated
3. smooth. : involuntary : Non Striated

Striated muscle is composed of

- the sarcolemma.
- myofibrils
An individual muscle fiber cell, which may
extend the entire length of the muscle
The Sarcoplasm
Within this fluid is contained
- glycogen,
- the high-energy compounds ATP
- phosphocreatine, and
- the enzymes of glycolysis.

The structure of voluntary muscle.

B. Contracted

The major protein of muscle

1. Actin : - G- actin

- F- actin

2. Myosin : contributes 55% of muscle protein by weight

and forms the thick filaments
- Heavy (H) chains --- one pair
- Light (L) chains ---- two pairs

In striated muscle, there are two other proteins

-Tropomyosin is a fibrous molecule that consists of

two chains,alpha and beta, that attach to -actin in
the groove between its filaments
Tropomyosin is present in all muscular and musclelike structures.
- Troponin complex is unique to striated muscle and
consists of three polypeptides.
1. Troponin T (TpT) binds to tropomyosin as well
as to the other two troponin components.

2. Troponin I (TpI) inhibits the F-actin-myosin

interaction and also binds to the other
components of troponin.
3. Troponin C (TpC) is a calcium- binding
polypeptide
that is structurally and functionally analogous
to calmodulin, animportant calcium-binding
protein widely distributed in nature.

Four molecules of calcium ion are bound per

molecule of troponin C or calmodulin, and both
molecules have a molecular mass of 17 kDa.

Myosin molecule showing the two intertwined

- - -helices (fibrous portion),
- the globular region or head (G),
- the light chains (L), and
- the effects of proteolytic cleavage by
trypsin and papain.
The globular region (myosin head) contains an
actin-binding site and an L chain-binding site
and also attaches to the remainder of the
myosin molecule.

skeletal, cardiac, and smooth muscle.

The major biochemical events occurring during

one cycle of muscle contraction and relaxation
(1) In the relaxation phase of muscle contraction,
the S-1 head of myosin hydrolyzes ATP to ADP and Pi,
but these products remain bound. The resultant ADPPi- myosin complex has been energized and is in a so
called high-energy conformation.
(2) When contraction of muscle is stimulated (via
events involving Ca2+, troponin, tropomyosin, and
actin, which are described below), actin becomes
accessible and the S-1 head of myosin finds it, binds
it, and forms the actin-myosin-ADP-Pi complex
indicated.

 (3) Formation of this complex promotes the

release of Pi, which initiates the power stroke.
This is Followed by release of ADP and is
accompanied by a large conformational change in
the head of myosin in relation to its tail , pulling
actin about 10 nm toward the center of the
sarcomere.
This is the power stroke.
The myosin is now in a so-called low-energy
state, indicated as actin- myosin

(4) Another molecule of ATP binds to the S1 head,forming an actin-myosin-ATP complex.

(5) Myosin-ATP has a low affinity for actin,

and actin is thus released.
This last step is a key component of
relaxation and is dependent upon the binding
of ATP to the actin-myosin complex.

The hydrolysis of ATP drives the cyclic

association and dissociation of actin and
myosin

The Contraction Process

Electrical signal arrives at the cell.
Electrical signal causes Ca2+ release into the
cell.
Ca2+ binds to troponin.
Troponin/Ca 2+ no longer binds actin.
Tropomyosin is no longer blocking the myosin
binding sites on actin.
Myosin binds actin.

ATP is hydrolyzed supplying the energy for the

myosin heads to move with respect to the rod
portion, causing the actin filaments to be drawn
towards the center of the sarcomere.
This process is repeated many times; with each
movement of a myosin head, the thin filament
pulled further inward.

White Fibers
Fast twitch
Large diameter, used for speed and strength.
Depends on the phosphagen system and on
glycolysis-lactic acid.
Stores glycogen for conversion to glucose.
Fewer blood vessels.
Little or no myoglobin.

Red Fibers
Slow twitch
Small diameter, used for endurance.
Depends on aerobic metabolism. Utilize fats as
well as glucose. Little glycogen storage. Many
blood vessels and much myoglobin give this
muscle its reddish appearance.

Sequence of events in contraction

and relaxation of skeletal muscle.
Steps in contraction
(1) Discharge of motor neuron
(2) Release of transmitter (acetylcholine) at
motor endplate
(3) Binding of acetylcholine to nicotinic
acetylcholine receptors
(4) Increased Na+ and K+ conductance in
endplate membrane
(5) Generation of endplate potential

 (6) Generation of action potential in muscle

fibers
(7) Inward spread of depolarization along T
tubules
(8) Release of Ca2+ from terminal cisterns
of sarcoplasmic reticulum and diffusion to
thick and thin filaments
(9) Binding of Ca2+ to troponin C, uncovering
myosin binding sites of actin
(10) Formation of cross-linkages between
actin and myosin and sliding of thin on thick
filaments, producing shortening

 Steps in relaxation
(1) Ca2+ pumped back into sarcoplasmic
reticulum
(2) Release of Ca2+ from troponin
(3) Cessation of interaction between actin
and myosin

Regulation of smooth muscle contraction by Ca2+. pLmyosin is the phosphorylated light chain of myosin; Lmyosin is the dephosphorylated light chain.

The multiple sources of ATP in muscle.

Characteristics of type I and type II

fibers of skeletal muscle.

Types of muscle fibers and major fuel sources

used by a sprinter and by a marathon
runner.

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