SKELETAL MUSCLE

LAB REPORT
Lauren Willey

Introduction:
The skeletal muscle is composed of intricate tissues that have a detailed structure and
voluntarily contract. An early anatomist in 1584 known as Andreas Vesalius,
contributed drawings of skeletal muscle to the world of anatomy. Skeletal muscles are
ultimately made up of myofibrils that contain thick and thin protein filaments called
myosin and actin. A.F Huxley and Niedergerke in 1954, are accredited founders of the
sliding filament theory which is essentially the basic mechanism for contraction of
those protein filaments in the skeletal muscle. In 1984, Ritchie and Woods researched
muscle fatigue, or motor deficit. It is the gradual exercise-induced decrease in the force
of a muscle as it performs contraction. Below are three labs that delve deeper into the
complex structure of the skeletal muscle and its responses to stimuli including ATP and
continuous and repetitive force.

Structure:

Figure 1. A skeletal muscle. Our tendons connect muscle to bone. Skeletal muscles have
an outer layer of epimysium covered by fascia. Making up skeletal muscles are made
up of fascicles covered by perimysium. Fascicles are composed of muscle fibers, which
are the cells. These fibers are covered by endonysium. The fibers have thousands of
striations. The area between the striations are called sarcomeres. Myofibrils make up
the muscle fibers. Inside the myofibrils are two main protein filaments myosin and
actin.

Muscle Contraction:
Width of rabbit muscle before solution
Width of muscle after
ATP and KCl
was added. Notice minute striations
and MgCl2 application. Notice

striations are scrunched together.

Length of rabbit muscle before solution

was added.

Length of rabbit muscle after

ATP
and KCl and MgCl2 application.

Figure 2.1
Muscle Fiber
Length (mm)

Before ATP
length

After ATP
length

Before ATP
width

After ATP
width

92mm

67mm

9mm

14mm

91mm

53mm

10mm

14mm

92mm

69mm

9mm

12mm

90mm

74mm

8mm

13mm

Averages

91.25mm

65.75mm

9mm

13.25mm

% Contraction

2.8%

91.25-65.75= 25.5 25.5/91.25= 2.8

-4.7%
9-13.25=-4.25 -4.25/9=-4.7
Figure 2.2

Figure 2.3
Figure 2.1, 2.2, 2.3. Photos and table 2.2 show the effects of ATP on muscle fibers. After
ATP was applied to the muscle fibers, their length got smaller and width became
thicker. Fig. 2.3 The percent of contraction of their length was 2.8, while the percent
contraction of the width was 4.7. Exposed binding sites on the actin filaments in
muscle fibers allow linkages to form between myosin heads and actin. These linkages
form cross-bridges. ATP breaks the myosin-actin cross-bridge that frees myosin for the
next contraction.
Table 1 - Continuous Grip
Time Interval

Maximum Force (N)

Maximum Force (N)

0-10 s

99.7N

20-30 s

92.8N

6.9N

40-50 s

57.9N

34.9N

60-70 s

51.0N

6.9N

80-90 s

29N

22N
Figure 3.1

Table 2 - Repetitive Grip

Time Interval

Maximum Force (N)

Maximum Force (N)

0-10 s

111.7N

20-30 s

61N

50.7N

40-50 s

89.7N

-28.7N

60-70 s

80.4N

9.3N

80-90 s

101.5N

-21.1N
Figure 3.2

Figure 3.1 &3.2. Contractability and fatigue depend on type of muscle fiber. There are
three types: slow oxidative, fast oxidative-glycolytic, and fast glycolytic. The amount of
force a muscle fiber develops depends on the number of myosin heads attached to
actin. Muscle fibers with a larger diameter develop more force because they contain
more myofibrils. The more myofibrils, the more myosin heads that can attach to actin.
The speed at which the contraction cycle can occur is determined by how fast myosin
ATPase can break down ATP. Fast glycolytic fibers and fast oxidative-glycolytic fibers
have a myosin ATPase that breaks down ATP faster than in slow oxidative fibers.
Muscle fatigue in constant grip occurred quicker than in repetitive grip. Slow oxidative
muscle fibers breaks down ATP slower, resulting in slower contraction cycles.
Although fast glycolytic and fast oxidative-glycolytic fibers have faster contraction
cycles, they produce ATP through glycolysis which can produce ATP quickly, but not
large amounts over time. This is what causes muscle fatigue. On the other hand, slow
oxidative muscle fibers use aerobic respiration which take longer to fatigue.

3D drawing of fascicle with one protruding muscle fiber and myofibrils that make up
those cells.