7.1 Haemoglobin Flashcards
(256 cards)
1
Q
what is the role of haemoglobin?
A
to transport oxygen around the body
2
Q
do all organisms have the same type of haemoglobin?
A
no
3
Q
What is haemoglobin made out of?
A
4 polypeptide chains with an Fe iron-containing haem group centre
4
Q
which metal ion is at the centre of the haemoglobin molecule?
A
Fe
5
Q
in what cell would you find haemoglobin?
A
red blood cell
6
Q
define haemoglobin
A
globular protein in blood that readily combines with oxygen to transport it around the body.
7
Q
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
A
it makes it easier
8
Q
describe the primary structure of haemoglobin
A
sequence of amino acids in the four polypeptide chains
9
Q
describe the secondary structure of haemoglobin
A
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix
10
Q
describe the tertiary structure of haemoglobin
A
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
11
Q
describe the quaternary structure of haemoglobin
A
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
12
Q
what does low affinity correlate with in terms of dissociation?
A
low affinity = high dissociation
13
Q
how does foetal haemoglobin differ?
A
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
14
Q
What is haemoglobin made out of?
A
4 polypeptide chains with an Fe iron-containing haem group centre
15
Q
define haemoglobin
A
globular protein in blood that readily combines with oxygen to transport it around the body.
16
Q
describe the primary structure of haemoglobin
A
sequence of amino acids in the four polypeptide chains
17
Q
describe the secondary structure of haemoglobin
A
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix
18
Q
describe the tertiary structure of haemoglobin
A
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
19
Q
describe the quaternary structure of haemoglobin
A
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
20
Q
what does low affinity correlate with in terms of dissociation?
A
low affinity = high dissociation
21
Q
how does foetal haemoglobin differ?
A
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
22
Q
What is haemoglobin made out of?
A
4 polypeptide chains with an Fe iron-containing haem group centre
23
Q
define haemoglobin
A
globular protein in blood that readily combines with oxygen to transport it around the body.
24
Q
describe the primary structure of haemoglobin
A
sequence of amino acids in the four polypeptide chains
25
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
26
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
27
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
28
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
29
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
30
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
31
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
32
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
33
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
34
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
35
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
36
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
37
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
38
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
39
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
40
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
41
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
42
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
43
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
44
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
45
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
46
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
47
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
48
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
it makes it easier
49
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
50
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
51
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
52
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
53
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
54
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
55
do all organisms have the same type of haemoglobin?
no
56
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
57
which metal ion is at the centre of the haemoglobin molecule?
Fe
58
in what cell would you find haemoglobin?
red blood cell
59
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
60
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
it makes it easier
61
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
62
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
63
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
64
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
65
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
66
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
67
do all organisms have the same type of haemoglobin?
no
68
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
69
which metal ion is at the centre of the haemoglobin molecule?
Fe
70
in what cell would you find haemoglobin?
red blood cell
71
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
72
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
it makes it easier
73
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
74
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
75
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
76
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
77
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
78
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
79
do all organisms have the same type of haemoglobin?
no
80
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
81
which metal ion is at the centre of the haemoglobin molecule?
Fe
82
in what cell would you find haemoglobin?
red blood cell
83
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
84
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
it makes it easier
85
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
86
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
87
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
88
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
89
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
90
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
91
what is the process by which haemoglobin associates with oxygen called?
loading, or associating
92
where does loading/associating of haemoglobin with oxygen take place in humans
the lungs
93
what is the process by which haemoglobin releases its oxygen called?
unloading, or dissociating
94
where does unloading/dissociating of haemoglobin with oxygen take place in humans?
the tissues
95
what happens when haemoglobin has a high affinity for oxygen
takes up oxygen more easily
| but release it less easily
96
what happens when haemoglobin has a low affinity for oxygen?
takes up oxygen less easily
| but release it more easily
97
to be efficient at transporting oxygen, haemoglobin must...
readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.
98
do all organisms have the same type of haemoglobin?
no
99
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
100
which metal ion is at the centre of the haemoglobin molecule?
Fe
101
in what cell would you find haemoglobin?
red blood cell
102
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
103
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
it makes it easier
104
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
105
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
106
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
107
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
108
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
109
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
110
what is the process by which haemoglobin associates with oxygen called?
loading, or associating
111
where does loading/associating of haemoglobin with oxygen take place in humans
the lungs
112
what is the process by which haemoglobin releases its oxygen called?
unloading, or dissociating
113
where does unloading/dissociating of haemoglobin with oxygen take place in humans?
the tissues
114
what happens when haemoglobin has a high affinity for oxygen
takes up oxygen more easily
| but release it less easily
115
what happens when haemoglobin has a low affinity for oxygen?
takes up oxygen less easily
| but release it more easily
116
to be efficient at transporting oxygen, haemoglobin must...
readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.
117
do all organisms have the same type of haemoglobin?
no
118
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
119
which metal ion is at the centre of the haemoglobin molecule?
Fe
120
in what cell would you find haemoglobin?
red blood cell
121
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
122
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
it makes it easier
123
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
124
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
125
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
126
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
127
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
128
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
129
what is the process by which haemoglobin associates with oxygen called?
loading, or associating
130
where does loading/associating of haemoglobin with oxygen take place in humans
the lungs
131
what is the process by which haemoglobin releases its oxygen called?
unloading, or dissociating
132
where does unloading/dissociating of haemoglobin with oxygen take place in humans?
the tissues
133
what happens when haemoglobin has a high affinity for oxygen
takes up oxygen more easily
| but release it less easily
134
what happens when haemoglobin has a low affinity for oxygen?
takes up oxygen less easily
| but release it more easily
135
to be efficient at transporting oxygen, haemoglobin must...
readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.
136
haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?
changes shape in the presence of certain substances, such as carbon dioxide, the new shape of the haemoglobin molecule binds more loosely to oxygen.
as a result haemoglobin releases its oxygen
organism is able to adapt to its environment, e.g. mountains (low oxygen)
137
do all organisms have the same type of haemoglobin?
no
138
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
139
which metal ion is at the centre of the haemoglobin molecule?
Fe
140
in what cell would you find haemoglobin?
red blood cell
141
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
142
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
it makes it easier
143
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
144
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
145
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
146
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
147
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
148
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
149
what is the process by which haemoglobin associates with oxygen called?
loading, or associating
150
where does loading/associating of haemoglobin with oxygen take place in humans
the lungs
151
what is the process by which haemoglobin releases its oxygen called?
unloading, or dissociating
152
where does unloading/dissociating of haemoglobin with oxygen take place in humans?
the tissues
153
what happens when haemoglobin has a high affinity for oxygen
takes up oxygen more easily
| but release it less easily
154
what happens when haemoglobin has a low affinity for oxygen?
takes up oxygen less easily
| but release it more easily
155
to be efficient at transporting oxygen, haemoglobin must...
readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.
156
haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?
changes shape in the presence of certain substances, such as carbon dioxide, the new shape of the haemoglobin molecule binds more loosely to oxygen.
as a result haemoglobin releases its oxygen
organism is able to adapt to its environment, e.g. mountains (low oxygen)
157
do all organisms have the same type of haemoglobin?
no
158
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
159
which metal ion is at the centre of the haemoglobin molecule?
Fe
160
in what cell would you find haemoglobin?
red blood cell
161
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
162
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
it makes it easier
163
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
164
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
165
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
166
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
167
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
168
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
169
what is the process by which haemoglobin associates with oxygen called?
loading, or associating
170
where does loading/associating of haemoglobin with oxygen take place in humans
the lungs
171
what is the process by which haemoglobin releases its oxygen called?
unloading, or dissociating
172
where does unloading/dissociating of haemoglobin with oxygen take place in humans?
the tissues
173
what happens when haemoglobin has a high affinity for oxygen
takes up oxygen more easily
| but release it less easily
174
what happens when haemoglobin has a low affinity for oxygen?
takes up oxygen less easily
| but release it more easily
175
to be efficient at transporting oxygen, haemoglobin must...
readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.
176
haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?
changes shape in the presence of certain substances, such as carbon dioxide, the new shape of the haemoglobin molecule binds more loosely to oxygen.
as a result haemoglobin releases its oxygen
organism is able to adapt to its environment, e.g. mountains (low oxygen)
177
do all organisms have the same type of haemoglobin?
no
178
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
179
which metal ion is at the centre of the haemoglobin molecule?
Fe
180
in what cell would you find haemoglobin?
red blood cell
181
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
182
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
it makes it easier
183
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
184
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
185
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
186
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
187
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
188
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
189
what is the process by which haemoglobin associates with oxygen called?
loading, or associating
190
where does loading/associating of haemoglobin with oxygen take place in humans
the lungs
191
what is the process by which haemoglobin releases its oxygen called?
unloading, or dissociating
192
where does unloading/dissociating of haemoglobin with oxygen take place in humans?
the tissues
193
what happens when haemoglobin has a high affinity for oxygen
takes up oxygen more easily
| but release it less easily
194
what happens when haemoglobin has a low affinity for oxygen?
takes up oxygen less easily
| but release it more easily
195
to be efficient at transporting oxygen, haemoglobin must...
readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.
196
haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?
changes shape in the presence of certain substances, such as carbon dioxide, the new shape of the haemoglobin molecule binds more loosely to oxygen.
as a result haemoglobin releases its oxygen
organism is able to adapt to its environment, e.g. mountains (low oxygen)
197
do all organisms have the same type of haemoglobin?
no
198
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
199
which metal ion is at the centre of the haemoglobin molecule?
Fe
200
in what cell would you find haemoglobin?
red blood cell
201
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
202
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
it makes it easier
203
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
204
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
205
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
206
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
207
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
208
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
209
what is the process by which haemoglobin associates with oxygen called?
loading, or associating
210
where does loading/associating of haemoglobin with oxygen take place in humans
the lungs
211
what is the process by which haemoglobin releases its oxygen called?
unloading, or dissociating
212
where does unloading/dissociating of haemoglobin with oxygen take place in humans?
the tissues
213
what happens when haemoglobin has a high affinity for oxygen
takes up oxygen more easily
| but release it less easily
214
what happens when haemoglobin has a low affinity for oxygen?
takes up oxygen less easily
| but release it more easily
215
to be efficient at transporting oxygen, haemoglobin must...
readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.
216
haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?
changes shape in the presence of certain substances, such as carbon dioxide, the new shape of the haemoglobin molecule binds more loosely to oxygen.
as a result haemoglobin releases its oxygen
organism is able to adapt to its environment, e.g. mountains (low oxygen)
217
do all organisms have the same type of haemoglobin?
no
218
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
219
which metal ion is at the centre of the haemoglobin molecule?
Fe
220
in what cell would you find haemoglobin?
red blood cell
221
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
222
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
it makes it easier
223
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
224
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
225
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
226
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
227
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
228
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
229
what is the process by which haemoglobin associates with oxygen called?
loading, or associating
230
where does loading/associating of haemoglobin with oxygen take place in humans
the lungs
231
what is the process by which haemoglobin releases its oxygen called?
unloading, or dissociating
232
where does unloading/dissociating of haemoglobin with oxygen take place in humans?
the tissues
233
what happens when haemoglobin has a high affinity for oxygen
takes up oxygen more easily
| but release it less easily
234
what happens when haemoglobin has a low affinity for oxygen?
takes up oxygen less easily
| but release it more easily
235
to be efficient at transporting oxygen, haemoglobin must...
readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.
236
haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?
changes shape in the presence of certain substances, such as carbon dioxide, the new shape of the haemoglobin molecule binds more loosely to oxygen.
as a result haemoglobin releases its oxygen
organism is able to adapt to its environment, e.g. mountains (low oxygen)
237
do all organisms have the same type of haemoglobin?
no
238
What is haemoglobin made out of?
4 polypeptide chains with an Fe iron-containing haem group centre
239
which metal ion is at the centre of the haemoglobin molecule?
Fe
240
in what cell would you find haemoglobin?
red blood cell
241
define haemoglobin
globular protein in blood that readily combines with oxygen to transport it around the body.
242
how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?
it makes it easier
243
describe the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
244
describe the secondary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
| in which each of these polypeptide chains is coiled into a helix
245
describe the tertiary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
246
describe the quaternary structure of haemoglobin
sequence of amino acids in the four polypeptide chains,
in which each of these polypeptide chains is coiled into a helix,
in which each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen,
in which all four polypeptides are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group - which contains a ferrous (Fe^2+) ion.
each Fe^2+ ion can combine with a single oxygen molecule (O2), making a total of four O2 molecules that can be carried by a single haemoglobin molecule in humans
247
what does low affinity correlate with in terms of dissociation?
low affinity = high dissociation
248
how does foetal haemoglobin differ?
has a higher affinity for oxygen at a lower partial pressure, po2
achieves sufficient oxygen saturation at a lower po2
249
what is the process by which haemoglobin associates with oxygen called?
loading, or associating
250
where does loading/associating of haemoglobin with oxygen take place in humans
the lungs
251
what is the process by which haemoglobin releases its oxygen called?
unloading, or dissociating
252
where does unloading/dissociating of haemoglobin with oxygen take place in humans?
the tissues
253
what happens when haemoglobin has a high affinity for oxygen
takes up oxygen more easily
| but release it less easily
254
what happens when haemoglobin has a low affinity for oxygen?
takes up oxygen less easily
| but release it more easily
255
to be efficient at transporting oxygen, haemoglobin must...
readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.
256
haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?
changes shape in the presence of certain substances, such as carbon dioxide, the new shape of the haemoglobin molecule binds more loosely to oxygen.
as a result haemoglobin releases its oxygen
organism is able to adapt to its environment, e.g. mountains (low oxygen)
