Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

AS Biology > 7.1 Haemoglobin > Flashcards

7.1 Haemoglobin Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
1
Q

what is the role of haemoglobin?

A

to transport oxygen around the body

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

do all organisms have the same type of haemoglobin?

A

no

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

which metal ion is at the centre of the haemoglobin molecule?

A

Fe

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

in what cell would you find haemoglobin?

A

red blood cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

do all organisms have the same type of haemoglobin?

A

no

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

which metal ion is at the centre of the haemoglobin molecule?

A

Fe

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

in what cell would you find haemoglobin?

A

red blood cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
61
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
62
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
63
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
64
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
65
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
66
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
67
Q

do all organisms have the same type of haemoglobin?

A

no

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
68
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
69
Q

which metal ion is at the centre of the haemoglobin molecule?

A

Fe

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
70
Q

in what cell would you find haemoglobin?

A

red blood cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
71
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
72
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
73
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
74
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
75
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
76
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
77
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
78
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
79
Q

do all organisms have the same type of haemoglobin?

A

no

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
80
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
81
Q

which metal ion is at the centre of the haemoglobin molecule?

A

Fe

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
82
Q

in what cell would you find haemoglobin?

A

red blood cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
83
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
84
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
85
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
86
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
87
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
88
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
89
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
90
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
91
Q

what is the process by which haemoglobin associates with oxygen called?

A

loading, or associating

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
92
Q

where does loading/associating of haemoglobin with oxygen take place in humans

A

the lungs

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
93
Q

what is the process by which haemoglobin releases its oxygen called?

A

unloading, or dissociating

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
94
Q

where does unloading/dissociating of haemoglobin with oxygen take place in humans?

A

the tissues

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
95
Q

what happens when haemoglobin has a high affinity for oxygen

A

takes up oxygen more easily

but release it less easily

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
96
Q

what happens when haemoglobin has a low affinity for oxygen?

A

takes up oxygen less easily

but release it more easily

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
97
Q

to be efficient at transporting oxygen, haemoglobin must…

A

readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
98
Q

do all organisms have the same type of haemoglobin?

A

no

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
99
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
100
Q

which metal ion is at the centre of the haemoglobin molecule?

A

Fe

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
101
Q

in what cell would you find haemoglobin?

A

red blood cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
102
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
103
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

104
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

105
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

106
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

107
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

108
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

109
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

110
Q

what is the process by which haemoglobin associates with oxygen called?

A

loading, or associating

111
Q

where does loading/associating of haemoglobin with oxygen take place in humans

A

the lungs

112
Q

what is the process by which haemoglobin releases its oxygen called?

A

unloading, or dissociating

113
Q

where does unloading/dissociating of haemoglobin with oxygen take place in humans?

A

the tissues

114
Q

what happens when haemoglobin has a high affinity for oxygen

A

takes up oxygen more easily

but release it less easily

115
Q

what happens when haemoglobin has a low affinity for oxygen?

A

takes up oxygen less easily

but release it more easily

116
Q

to be efficient at transporting oxygen, haemoglobin must…

A

readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.

117
Q

do all organisms have the same type of haemoglobin?

A

no

118
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

119
Q

which metal ion is at the centre of the haemoglobin molecule?

A

Fe

120
Q

in what cell would you find haemoglobin?

A

red blood cell

121
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

122
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

123
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

124
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

125
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

126
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

127
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

128
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

129
Q

what is the process by which haemoglobin associates with oxygen called?

A

loading, or associating

130
Q

where does loading/associating of haemoglobin with oxygen take place in humans

A

the lungs

131
Q

what is the process by which haemoglobin releases its oxygen called?

A

unloading, or dissociating

132
Q

where does unloading/dissociating of haemoglobin with oxygen take place in humans?

A

the tissues

133
Q

what happens when haemoglobin has a high affinity for oxygen

A

takes up oxygen more easily

but release it less easily

134
Q

what happens when haemoglobin has a low affinity for oxygen?

A

takes up oxygen less easily

but release it more easily

135
Q

to be efficient at transporting oxygen, haemoglobin must…

A

readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.

136
Q

haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?

A

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
Q

do all organisms have the same type of haemoglobin?

A

no

138
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

139
Q

which metal ion is at the centre of the haemoglobin molecule?

A

Fe

140
Q

in what cell would you find haemoglobin?

A

red blood cell

141
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

142
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

143
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

144
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

145
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

146
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

147
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

148
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

149
Q

what is the process by which haemoglobin associates with oxygen called?

A

loading, or associating

150
Q

where does loading/associating of haemoglobin with oxygen take place in humans

A

the lungs

151
Q

what is the process by which haemoglobin releases its oxygen called?

A

unloading, or dissociating

152
Q

where does unloading/dissociating of haemoglobin with oxygen take place in humans?

A

the tissues

153
Q

what happens when haemoglobin has a high affinity for oxygen

A

takes up oxygen more easily

but release it less easily

154
Q

what happens when haemoglobin has a low affinity for oxygen?

A

takes up oxygen less easily

but release it more easily

155
Q

to be efficient at transporting oxygen, haemoglobin must…

A

readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.

156
Q

haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?

A

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
Q

do all organisms have the same type of haemoglobin?

A

no

158
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

159
Q

which metal ion is at the centre of the haemoglobin molecule?

A

Fe

160
Q

in what cell would you find haemoglobin?

A

red blood cell

161
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

162
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

163
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

164
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

165
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

166
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

167
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

168
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

169
Q

what is the process by which haemoglobin associates with oxygen called?

A

loading, or associating

170
Q

where does loading/associating of haemoglobin with oxygen take place in humans

A

the lungs

171
Q

what is the process by which haemoglobin releases its oxygen called?

A

unloading, or dissociating

172
Q

where does unloading/dissociating of haemoglobin with oxygen take place in humans?

A

the tissues

173
Q

what happens when haemoglobin has a high affinity for oxygen

A

takes up oxygen more easily

but release it less easily

174
Q

what happens when haemoglobin has a low affinity for oxygen?

A

takes up oxygen less easily

but release it more easily

175
Q

to be efficient at transporting oxygen, haemoglobin must…

A

readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.

176
Q

haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?

A

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
Q

do all organisms have the same type of haemoglobin?

A

no

178
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

179
Q

which metal ion is at the centre of the haemoglobin molecule?

A

Fe

180
Q

in what cell would you find haemoglobin?

A

red blood cell

181
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

182
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

183
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

184
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

185
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

186
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

187
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

188
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

189
Q

what is the process by which haemoglobin associates with oxygen called?

A

loading, or associating

190
Q

where does loading/associating of haemoglobin with oxygen take place in humans

A

the lungs

191
Q

what is the process by which haemoglobin releases its oxygen called?

A

unloading, or dissociating

192
Q

where does unloading/dissociating of haemoglobin with oxygen take place in humans?

A

the tissues

193
Q

what happens when haemoglobin has a high affinity for oxygen

A

takes up oxygen more easily

but release it less easily

194
Q

what happens when haemoglobin has a low affinity for oxygen?

A

takes up oxygen less easily

but release it more easily

195
Q

to be efficient at transporting oxygen, haemoglobin must…

A

readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.

196
Q

haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?

A

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
Q

do all organisms have the same type of haemoglobin?

A

no

198
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

199
Q

which metal ion is at the centre of the haemoglobin molecule?

A

Fe

200
Q

in what cell would you find haemoglobin?

A

red blood cell

201
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

202
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

203
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

204
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

205
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

206
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

207
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

208
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

209
Q

what is the process by which haemoglobin associates with oxygen called?

A

loading, or associating

210
Q

where does loading/associating of haemoglobin with oxygen take place in humans

A

the lungs

211
Q

what is the process by which haemoglobin releases its oxygen called?

A

unloading, or dissociating

212
Q

where does unloading/dissociating of haemoglobin with oxygen take place in humans?

A

the tissues

213
Q

what happens when haemoglobin has a high affinity for oxygen

A

takes up oxygen more easily

but release it less easily

214
Q

what happens when haemoglobin has a low affinity for oxygen?

A

takes up oxygen less easily

but release it more easily

215
Q

to be efficient at transporting oxygen, haemoglobin must…

A

readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.

216
Q

haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?

A

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
Q

do all organisms have the same type of haemoglobin?

A

no

218
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

219
Q

which metal ion is at the centre of the haemoglobin molecule?

A

Fe

220
Q

in what cell would you find haemoglobin?

A

red blood cell

221
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

222
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

223
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

224
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

225
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

226
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

227
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

228
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

229
Q

what is the process by which haemoglobin associates with oxygen called?

A

loading, or associating

230
Q

where does loading/associating of haemoglobin with oxygen take place in humans

A

the lungs

231
Q

what is the process by which haemoglobin releases its oxygen called?

A

unloading, or dissociating

232
Q

where does unloading/dissociating of haemoglobin with oxygen take place in humans?

A

the tissues

233
Q

what happens when haemoglobin has a high affinity for oxygen

A

takes up oxygen more easily

but release it less easily

234
Q

what happens when haemoglobin has a low affinity for oxygen?

A

takes up oxygen less easily

but release it more easily

235
Q

to be efficient at transporting oxygen, haemoglobin must…

A

readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.

236
Q

haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?

A

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
Q

do all organisms have the same type of haemoglobin?

A

no

238
Q

What is haemoglobin made out of?

A

4 polypeptide chains with an Fe iron-containing haem group centre

239
Q

which metal ion is at the centre of the haemoglobin molecule?

A

Fe

240
Q

in what cell would you find haemoglobin?

A

red blood cell

241
Q

define haemoglobin

A

globular protein in blood that readily combines with oxygen to transport it around the body.

242
Q

how does one oxygen molecule binding to haemoglobin affect the binding of other molecules?

A

it makes it easier

243
Q

describe the primary structure of haemoglobin

A

sequence of amino acids in the four polypeptide chains

244
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

245
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

246
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

247
Q

what does low affinity correlate with in terms of dissociation?

A

low affinity = high dissociation

248
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

249
Q

what is the process by which haemoglobin associates with oxygen called?

A

loading, or associating

250
Q

where does loading/associating of haemoglobin with oxygen take place in humans

A

the lungs

251
Q

what is the process by which haemoglobin releases its oxygen called?

A

unloading, or dissociating

252
Q

where does unloading/dissociating of haemoglobin with oxygen take place in humans?

A

the tissues

253
Q

what happens when haemoglobin has a high affinity for oxygen

A

takes up oxygen more easily

but release it less easily

254
Q

what happens when haemoglobin has a low affinity for oxygen?

A

takes up oxygen less easily

but release it more easily

255
Q

to be efficient at transporting oxygen, haemoglobin must…

A

readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it.

256
Q

haemoglobin is able to change its affinity (chemical attraction) for oxygen under different conditions, how is this useful?

A

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)

AS Biology (66 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions