BGYB30 Midterm 2004 • Total number of Marks available= 56 • I will record all of the grades out of 54 total marks. • Small adjustment of +0.5 for different markers • Average mark = 36.4 • Class average after adjustments = 36.4 / 54 = 67.4%
Jan 29, 2016
BGYB30 Midterm 2004
• Total number of Marks available= 56
• I will record all of the grades out of 54 total marks.
• Small adjustment of +0.5 for different markers
• Average mark = 36.4
• Class average after adjustments = 36.4 / 54 = 67.4%
BGYB30 Midterm 2004
• Short Answers• Available for pickup next week during TA
office hours (Mon 10-12, Wed 12-1)
• If you want your test remarked– Compare your grade to posted marking scheme– Tests will be entirely remarked /56– Your test must NOT leave the office– All requests submitted by 1pm Nov 18
Taste Smell
Taste Smell
• Long distance• Many receptors
– 1000s mouse– 100-200 human
• All receptors are G-protein coupled receptors
• Depolarize olfactory cells, leading to APs
• Each receptor cell has only one or two types of receptor molecules
• Contact• 4 basic tastes
– Salt, bitter, sweet, sour– Complex mixing for taste
perception
• All modify synaptic transmission between taste receptor and a sensory neuron
• Individual receptor cells respond best to one type of taste and less well to others
Sensory neuron
depolarization
Ca++
Na+
Complex stimuliSugarsBitter
Ionic stimuliSalt (Na+)Sour (H+)
Second messenger
Intracellular Ca++
Taste Receptor
Olfaction
Press Release: The 2004 Nobel Prize in Physiology or Medicine4 October 2004
The Nobel Assembly at Karolinska Institutet has today decided to award The Nobel Prize in Physiology or Medicine for 2004
jointly to Richard Axel and Linda B. Buck
for their discoveries of "odorant receptors and the organization of the olfactory system"
ATP cAMP
Odourant molecule
G-proteinreceptor
Na+
glomerulus
Olfactory receptor cells with different receptor molecules
Taste & Smell
• Summary– Both are receive and process external
chemical stimuli– Taste receptors modify synaptic transmission– Olfactory receptors generate APs– Many types of olfactory receptors, only a few
types of taste receptors
MuscleNext Class: BGYB30 Pose-Off
Winner 2002
Winner 2003
Muscle
Striated Smooth
Skeletal•movement
Cardiac•heart
Blood vesselslungs
intestine
•Mechanisms of muscle contraction essentially the same
•Differences in how muscle cells are organized and how contractions initiated
MuscleTendon
Bone
Muscle Fibers
nucleus
Myofibril
Skeletal muscle
Z Z ZM
Sarcomere (2-3 m)
Aband
I
H
Myofibril
band
zone
Banding patterns due to overlapping protein filaments
H
A I
Z disk
Actinfilament
Myosinfilament
Actinfilament
‘cross bridges’
• When muscle contracts the sarcomere length is reduced
REST
CONTRACTION
STRETCH
• Length of filaments doesn’t change
• but the degree of overlap doessliding filament hypothesis
The degree of overlap is important for generating tensionSpecifically the number of cross-bridges
Stimulator
Sarcomere length (m)
Rel
ativ
e te
nsio
n
1.25 1.65 2 2.25 3.65
1.0
0.5
Control musclelength
Length – Tension relationship for single sarcomere
Measuretension
Sarcomere length (m)
Rel
ativ
e te
nsio
n
1.25 1.65 2 2.25 3.65
1.0
0.5
5
4
3 2
1
1
2
3
4
5
• At maximum stretch no overlap
• At peak tension optimal overlap
• As sarcomere shortens filaments interfere
Summary
• Muscles made of myofibrils• Myofibrils have sarcomeres
Functional unit of muscle contraction
• Thick and thin filaments give a banding pattern (myosin and actin)
• With contraction sarcomere length changes
• Maximum tension produced with optimal overlap of filaments
Next ClassBGYB30 Pose-Off
Winner 2002
Winner 2003
Myosin
Tail• assembles into filaments
Head • binds Actin• ATPase
Myosin Light ChainsS2 Link
protein filaments of the sarcomere
Actinfilament
Myosinfilament
Actinfilament
‘cross bridges’
Myosin filament
~150 cross-bridges at each end of the myosin filament
Myosin self-assembles into filaments
Actin filaments
• F-Actin (flimanetous) assembles from G-actin (globular)• Actin has myosin binding sites
Myofilament chemistry
Actin + myosin Actomyosin complex
Actin + myosin Actomyosin complexATP
Myosin-ATP Myosin-ADP-Pi Myosin +ADP +Pi
Myosin-ADP-Pi + Actin Actomyosin + ADP + Pi
Very slow!
Very fast!
Releases energy
Actin rate of ATP hydrolysis by myosin
Myosin-ADP-Pi binds Actin weakly
Myosin-ADP Head rotates
ADP is released and ATP binds Myosin
Myosin-ATP released from Actin
Myosin hydrolyzes ATPADP+Pi
Myosin-ADP binds Actin strongly
Pi
Myosin-ATP
Actin-Myosin Cycle
• Transition between weakly bound and strongly bound complex generates tension
Myosin filament
Myosin head group
S2 link
Actin filament Binding sites
Stretching of the link generates tension
Weakbinding
Strongbinding
Equal and opposite forceon thick filament
Why do thin filaments move?
Net forceNet force
Actin + myosin Actomyosin complexATP
What if we don’t have this?
X
Rigor mortis
Role of calcium• Intracellular Calcium is required for muscle
contraction
• Used ‘skinned’ muscle fibers
• Membranes chemically removed
• just protein components left
Calcium concentration (mM)
Rel
ativ
e fo
rce
1.0
0.01 0.1 1.0
Role of calcium
Troponin complex
Tropomyosin
•Troponin and Tropomyosin bind to actinblock the actin – myosin binding sites
•Troponin is a calcium binding protein
• When Troponin binds calcium it moves Tropomyosin away from the actin-myosin binding site
CaCa
Summary
• Myosin binds to Actin in ADP/ATP-dependent manner
• Transition from weak to strong bond rotates myosin head group
• Lengthening of the link generates tension
• Calcium is required to remove Troponin-Tropomyosin from the binding sites
Where does Calcium come from?
• Intracellular storage called Sarcoplasmic Reticulum
• Surround each myofibril of the whole muscle• Contains high concentration of calcium
• Transverse Tubules connects plasma membrane to deep inside muscle
Text Fig 10-21Myofibril
Sarcoplasmic Reticulum
Transverse tubules
Transverse tubules