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Sandbox max quiz

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<quiz display=simple>
<quiz display=simple>
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{If the amino acid sequence of a protein is reversed (the primary structure is the same except from N to C it now reads C to N) will the protein fold to the same tertiary structure?
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{If the amino acid sequence of a protein is reversed (the primary structure is the same except from N to C it now reads C to N) the protein will fold to the same tertiary structure.
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|type="()"}
- true
- true
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{
{
|type="{}"}
|type="{}"}
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Name an awesome 20th century physicist.
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Name an amino acid likely to be used in binding a metallic cationic cofactor.
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{ Heisenberg|Oppenheimer|Einstein|Curie|Max Planck|Max Leabo }
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{ aspartic acid|histidine|glutamic acid|asparagine|glutamine|Max Leabo }
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|| The negative charge for some, while the electronegative components for others has the potential to bind to positively charged cations.
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{Things are not as they seem
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{Some common techniques used by proteins to link hydrophobic and hydrophilic regions are
|type="[]"}
|type="[]"}
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- Correct answer.
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- relying on dissolved amphipathic molecules to shield exposed hydrophobic residues from the cytosol.
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+ Incorrect answer.
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+ stacking beta sheets with alternating hydrophobic and hydrophilic residues.
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- Correct answer.
+
- replacing the functional group on amino acid residues with more energetically favorable groups.
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+ Incorrect answer.
+
+ varying the order of hydrophobic and hydrophilic residues on an alpha helix so that the two types are segregated to opposite sides of the helix.
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||Ha Ha
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{ Which of these has a single domain? }
{ Which of these has a single domain? }

Current revision

See full explanation and examples on How To Use at Help:Quiz

1. If the amino acid sequence of a protein is reversed (the primary structure is the same except from N to C it now reads C to N) the protein will fold to the same tertiary structure.

true
false
→ The primary protein structure is directional because of the asymmetrical nature of amino acids. This causes potentially different molecular interactions depending on the order of the amino acid sequence and results in a different tertiary structure.

2. Which scene most likely highlights the hydrophobic sections of the protein:

Insert caption here

Drag the structure with the mouse to rotate

Insert caption here

Drag the structure with the mouse to rotate

Insert caption here

Drag the structure with the mouse to rotate
→ The first scene highlights a number of residues on the inner section of the protein. The location of these residues suggests they are hydrophobic

3.

Name an amino acid likely to be used in binding a metallic cationic cofactor.
→ The negative charge for some, while the electronegative components for others has the potential to bind to positively charged cations.

4. Some common techniques used by proteins to link hydrophobic and hydrophilic regions are

relying on dissolved amphipathic molecules to shield exposed hydrophobic residues from the cytosol.
stacking beta sheets with alternating hydrophobic and hydrophilic residues.
replacing the functional group on amino acid residues with more energetically favorable groups.
varying the order of hydrophobic and hydrophilic residues on an alpha helix so that the two types are segregated to opposite sides of the helix.

5. Which of these has a single domain?

[[

Insert caption here

Drag the structure with the mouse to rotate
]]
[[

Insert caption here

Drag the structure with the mouse to rotate
]]
[[

Insert caption here

Drag the structure with the mouse to rotate
]]
[[

Insert caption here

Drag the structure with the mouse to rotate
]]

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