Figure 932aAmyloid fibrils' a An electron micrograph of amyloid fibrils of the protein PrP 2730'

1
Figure 9-32a Amyloid fibrils. (a) An electron
micrograph of amyloid fibrils of the protein PrP
27-30.
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Figure 9-32bc Amyloid fibrils. (b) and (c) Model
and isolated b sheet.
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3
Figure 9-34a Evidence that the scrapie agent is a
protein.(a) Scrapie agent is inactivated by
treatment with diethylpyrocarbonate, which reacts
with His side chains.
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Figure 9-34b Evidence that the scrapie agent is a
protein.(b) Scrapie agent is unaffected by
treatment with hydroxylamine, which reacts with
cystosine residues.
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Figure 9-34c Evidence that the scrapie agent is a
protein.(c) Hydroxylamine rescues
diethylpyrocarbonate-inactivated scrapie reagent.
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Figure 9-35a Prion protein conformations. (a) The
NMR structure of human prion protein (PrPC).
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Figure 9-35b Prion protein conformations. (b) A
plausible model for the structure of PrPSc.
8
Heme proteins structure and function
9
Figure 9-36 Molecular formula for
iron-protoporphyrin IX (heme).
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Figure 9-37 Primary structures of some
representative c-type cytochromes.
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Figure 9-38 Three-dimensional structures of the
c-type cytochromes whose primary structures are
displayed in Fig. 9-37.
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Oxygen is transported to cells
which are remote from air

O2 is required in cells, in the mitochondria for
ATP production
aerobic metabolism
Glucose O2 ----------------------------gt ATP
CO2
oxidative phosphorylation
13
Oxygen is transported down
a concentration gradient
pO2
torr
14
lungs
BPG.CO
.
H
.
Hb 4O
ltgt Hb.(O
)

H

CO
BPG


BPG.CO
.
Hb 4O
ltgt Hb.(O
)

CO
BPG
H
.
H



2
2
2
4
2
2
2
2
4
2
O

H
,
CO

2
2
tissues
Hb.(O
)

CO
BPG ltgt BPG.CO
.
Hb 4O
H

H
.


Hb.(O
)

H

CO
BPG ltgt BPG.CO
.
H
.
Hb 4O


2
4
2
2
2
2
4
2
2
2
muscle cell membrane
Mb

O
ltgt Mb.O
Mb

O
ltgt Mb.O
2
2
2
2
mitochondria
Mb.O
ltgt Mb

O
Mb.O
ltgt Mb

O
2
2
2
2
15
Figure 10-11 Structure of sperm whale myoglobin.
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16
heme
myoglobin
proximal His (bound to Fe)
17
Figure 10-1 The heme group.
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Figure 10-2 The visible absorption spectra of
oxygenated and deoxygenated hemoglobins.
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(No Transcript)
20
proximal His
21
P50 2.8 torr
22
Fraction of Mb bound to O2 at pO2 30 torr
pO2 in capillaries
P50 2.8 torr
23
Figure 8-42a The X-Ray structure of horse heart
cytochrome.
24
myoglobin single subunit
hemoglobin four homologous subunits two alpha
two beta chains
25
Table 10-1a The Amino Acid Sequences of the a and
b Chains of Human Hemoglobin and of Human
Myoglobina,b
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Table 10-1b The Amino Acid Sequences of the a and
b Chains of Human Hemoglobin and of Human
Myoglobina,b
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27
Figure 10-3 Oxygen dissociation curves of Mb and
of Hb in whole blood.
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Non-cooperative binding
Cooperative binding
29
About 33 of O2 delivered
30
About 42 of O2 delivered
31
Figure 10-5 A picket-fence Fe(II)porphyrin
complex with bound O2.
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32
Figure 10-7 Comparison of the O2-dissociation
curves of stripped Hb and whole blood in 0.01M
NaCl at pH 7.0.
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Figure 10-13a The X-ray structure of deoxyHb as
viewed down its exact 2-fold axes.
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34
Figure 10-13b The X-ray structure of oxyHb as
viewed down its exact 2-fold axes.
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35
Oxy-Hb R State
Deoxy-Hb T State
VVP Fig 7-5
36
Figure 10-14 The major structural differences
between the quaternary conformations of (a)
deoxyHb and (b) oxyHb.
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Figure 10-15 The heme group and its environment
in the unliganded a chain of human Hb.
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Figure 10-16 Triggering mechanism for the T R
transition in Hb.
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Figure 10-17 The a1Cb2FG interface of Hb in (a)
the T state and (b) the R state.
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Figure 10-18 The hemoglobin a1b2 interface as
viewed perpendicularly to Fig. 10-13.
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