Muscle structure & training principles Flashcards
1
Q
muscle structure
A
contractile proteins
- myosin: thick filaments with globular heads
- actin: thin filaments
(actin, tropomyosin, troponin)
2
Q
mechanisms of muscle contraction
A
- Myosin head binds to an active site on actin (‘cross bridge’)
- Myosin head moves pulling actin filaments towards the centre of the sarcomere (‘power stroke’)
- Sacromere shortens, muscle shortens, force is generated
- Cross bridges detach
- Dependent upon sufficient Ca2+ and ATP
3
Q
sliding filament theory
A
- ATP is hydrolysed when myosin head is unattached
- troponin-Ca2+ complex pulls tropomyosin away, exposing myosin binding sites - ADP + Pi are bound to myosin as myosin head attaches to actin
- ADP + Pi release causes head to change position and acting filament to move
- binding of ATP causes myosin head to return to resting position
4
Q
role of Ca2+ in muscle contraction
A
- At rest, myosin and actin are unable to bind d/t tropomyosin and troponin
o Tropomyosin covers the binding sites on actin
o Troponin holds tropomyosin in place - Ca2+ binds to troponin moves tropomyosin away to expose myosin binding site on actin
5
Q
role of ATP in muscle contraction
A
- Myosin head contains a binding site for ATP
- ATP –> ADP + P = cross bridge + power stroke
- A new ATP binds to myosin to release it from actin
6
Q
excitation-contraction coupling
A
Sequence of events that begin with a neural impulse and end with contraction
- Excitation of a motor nerve
- Propagation of an action potential
- Events at the neuromuscular junction
- Calcium release from sarcoplasmic reticulum
- Sliding Filament Theory
- Muscle contraction
7
Q
muscle fibre types
A
- Type I fibres (slow twich)
-Type II fibres (fast twitch)
o Type IIa
o Type IIx (IIb) - Differences in speed of contraction, maximum force production, oxidative capacity, fatigability…
- Power production is the key determinant of recruitment
8
Q
Type I
A
- Relatively small in diameter
- Slow contractile speed
- Low force production
- High oxidative (aerobic) capacity o Many mitochondria o Many capillaries o Lots of myoglobin o Great aerobic enzyme activity
- Highly resistant to fatigue
- Dominant muscle fibre during exercise below CP
9
Q
Type II
A
- Relatively large in diameter
- Fast contractile speed
- High force production
- High glycolytic capacity
o Lots of glycolytic enzymes
o Greater glycogen and PCr stores - Highly fatigable
- Recruited during high-intensity exercise
10
Q
Type IIa
A
- Moderately well-developed oxidative capacity
o Many mitochondria
o Moderate number of capillaries - Gradually recruited during exercise bouts >CP
o i.e. High intensity aerobic exercise <40min – 1hr. Typical anaerobic exercise bouts
11
Q
Type IIx(b)
A
- Largely anaerobic o High contractile speed, force, power o Great glycolytic capacity o High concentration of CP o Slight oxidative capacity o Highly fatigable
- Recruited during short (<1min), very high-intensity anaerobic exercise, when requirement for force and/or speed is high
12
Q
distribution of fibre types
A
- Skeletal muscle contain both type I and type II fibres however the proportion of these fibres differ
- Postural muscles – higher proportion of type I
- Power muscles – higher proportion of type II
- e.g. Gastrocnemius vs. Soleus
13
Q
determinants of fibre type
A
- Genetics ~50%
- Environment ~50%: Training, physical inactivity
- Significant differences between individuals
14
Q
assessment of fibre types (muscle biopsy)
A
- Site is anaesthetised
- Small incision is made (1-3cm)
- Needle is inserted into the muscle
- 10-100mg sample is extracted (~grain of rice)
o Not too big to reduce impact on performance - Samples from metabolically active sites
o e.g. deltoids in swimmers - Sample is stained to identify fibre type
15
Q
purpose of training
A
- Improvements in health and performance o Cardiorespiratory fitness o Muscular strength and endurance o Body composition o Flexibility o Speed o Agility o Power - Adaptation: Key to training