User:Eric Martz/Hemoglobin Quiz

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||
-
{qqq
+
{Molecular oxygen binds directly to, and is released from
|type="[]"}
|type="[]"}
-
+ aaa.
+
- alpha helices
 +
- oxygen atoms
 +
+ histidine amino acids
 +
- cysteine amino acids
 +
+ iron atoms
 +
- magnesium atoms
||
||
-
{qqq
+
{Heme groups are held
|type="[]"}
|type="[]"}
-
+ aaa.
+
+ in alpha chains
 +
+ in beta chains
 +
- between alpha and beta chains
 +
- in gamma chains
||
||
-
{qqq
+
{More than half of the atoms in heme are
|type="[]"}
|type="[]"}
-
+ aaa.
+
+ carbon
 +
- oxygen
 +
- nitrogen
 +
- sulfur
||
||
-
{qqq
+
{Hydrogen bonds
|type="[]"}
|type="[]"}
-
+ aaa.
+
- are covalent bonds
 +
+ are non-covalent bonds
 +
- form between two hydrogen atoms
 +
+ stabilize the main chain conformation in alpha helices
||
||
-
{qqq
+
{Each chain in the hemoglobin molecule contains
|type="[]"}
|type="[]"}
-
+ aaa.
+
- multiple beta strands
 +
+ multiple alpha helices
 +
- a hydrophilic core
 +
+ a hydrophobic core
 +
+ one pocket to hold one heme
 +
- one pocket to hold two hemes
||
||
-
{qqq
+
{An amphipathic alpha helix is one that
|type="[]"}
|type="[]"}
-
+ aaa.
+
- occurs only in sickle disease
 +
- occurs only in the de-oxy form of hemoglobin
 +
- is hydrophilic on both sides
 +
+ has a hydrophilic side and a hydrophobic side
 +
- is hydrophobic on both sides
||
||
-
{qqq
+
{Amino acids with hydrophobic sidechains are present mostly
|type="[]"}
|type="[]"}
-
+ aaa.
+
+ where they do not contact water
 +
- on the surface of the protein molecule
 +
- in order to bind molecular oxygen
 +
+ buried in the center of the protein molecule
 +
- in separate helices from the helices of hydrophilic amino acids
||
||
-
{qqq
+
{Salt bridges
|type="[]"}
|type="[]"}
-
+ aaa.
+
+ form when oppositely-charged amino acid sidechains contact each other
 +
- form when positively charged amino acid sidechains contact each other
 +
- form mostly in the core of the molecule
 +
+ form mostly on the surface of the molecule
 +
- are covalent bonds
||
||
 +
 +
{Histidine amino acids
 +
|type="[]"}
 +
- have oxygen in their sidechains
 +
+ have nitrogen in their sidechains
 +
+ have carbon in their sidechains
 +
+ bind tightly to Fe++
 +
+ help to bind molecular oxygen
 +
 +
Oxygen binding
 +
|type="[]"}
 +
+ is partly to a histidine sidechain nitrogen
 +
+ moves the iron in heme
 +
+ changes the conformation of hemoglobin
 +
+ is stronger at the higher pH in the lungs
 +
+ causes some salt bridges to separate
 +
+ is decreased by diphosphoglyceric acid
 +
 +
Sickle hemoglobin
 +
|type="[]"}
 +
+is advantageous in some parts of the world
 +
+shortens the lifetime of red blood cells
 +
+impairs blood flow
 +
+is caused by a mutation that changes a single amino acid
 +
+causes severe disease only in homozygotes
 +
+polymerizes into fibers due to hydrophobic interactions
 +
</quiz>
</quiz>

Revision as of 20:15, 16 September 2018

Hemoglobin Quiz

You will get immediate feedback when you click Submit. The quiz below is offered to accompany the interactive tutorial Hemoglobin Molecular Structure.

1.

The number of protein chains in each hemoglobin molecule is

2.

The number of heme-iron complexes in each hemoglobin molecule is

3.

When saturated, the number of oxygen atoms bound by one molecule of hemoglobin is
→ Number of oxygen ATOMS, not number of O2 molecules.

Questions below may have more than one correct answer.

4. The function of hemoglobin is

To pick up oxygen in the lungs.
To convert oxygen to carbon dioxide and water.
To transport oxygen.
To release oxygen in the lungs.
To release oxygen in body tissues.

5. The polypeptide chains that fit together to make one hemoglobin molecule are held together by

disulfide bonds
covalent bonds
non-covalent interactions
oxygen

6. The iron atom is held in place by direct contact with

carboxyl groups in heme
nitrogens in heme
carbons in heme
sulfur atoms in cysteines
nitrogen atoms in histidines
oxygen atoms in histidines

7. Molecular oxygen binds directly to, and is released from

alpha helices
oxygen atoms
histidine amino acids
cysteine amino acids
iron atoms
magnesium atoms

8. Heme groups are held

in alpha chains
in beta chains
between alpha and beta chains
in gamma chains

9. More than half of the atoms in heme are

carbon
oxygen
nitrogen
sulfur

10. Hydrogen bonds

are covalent bonds
are non-covalent bonds
form between two hydrogen atoms
stabilize the main chain conformation in alpha helices

11. Each chain in the hemoglobin molecule contains

multiple beta strands
multiple alpha helices
a hydrophilic core
a hydrophobic core
one pocket to hold one heme
one pocket to hold two hemes

12. An amphipathic alpha helix is one that

occurs only in sickle disease
occurs only in the de-oxy form of hemoglobin
is hydrophilic on both sides
has a hydrophilic side and a hydrophobic side
is hydrophobic on both sides

13. Amino acids with hydrophobic sidechains are present mostly

where they do not contact water
on the surface of the protein molecule
in order to bind molecular oxygen
buried in the center of the protein molecule
in separate helices from the helices of hydrophilic amino acids

14. Salt bridges

form when oppositely-charged amino acid sidechains contact each other
form when positively charged amino acid sidechains contact each other
form mostly in the core of the molecule
form mostly on the surface of the molecule
are covalent bonds

15. Histidine amino acids

have oxygen in their sidechains
have nitrogen in their sidechains
have carbon in their sidechains
bind tightly to Fe++
help to bind molecular oxygen
is partly to a histidine sidechain nitrogen
moves the iron in heme
changes the conformation of hemoglobin
is stronger at the higher pH in the lungs
causes some salt bridges to separate
is decreased by diphosphoglyceric acid
is advantageous in some parts of the world
shortens the lifetime of red blood cells
impairs blood flow
is caused by a mutation that changes a single amino acid
causes severe disease only in homozygotes
polymerizes into fibers due to hydrophobic interactions

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Eric Martz

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