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Sandbox max quiz 2

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<applet size='400' frame='true' align='right' caption='Morph: 2oau to 2vv5.'
<applet size='400' frame='true' align='right' caption='Morph: 2oau to 2vv5.'
scene='User:Eric_Martz/Sandbox_0/2oau_2vv5_morph_cao_pdb_gz/1' />
scene='User:Eric_Martz/Sandbox_0/2oau_2vv5_morph_cao_pdb_gz/1' />
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{Using the scene to the right showing the structure of E. coli McsS as well as the morph between the open and closed conformation, which side undergoes the most major conformational change.
{Using the scene to the right showing the structure of E. coli McsS as well as the morph between the open and closed conformation, which side undergoes the most major conformational change.
|type="()"}
|type="()"}
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+ Periplasmic
+ Periplasmic
|| Why might the smaller periplasmic side be the site of conformational shifting? What other functions might the cytoplasmic domain serve?
|| Why might the smaller periplasmic side be the site of conformational shifting? What other functions might the cytoplasmic domain serve?
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Revision as of 17:12, 15 April 2010

This is a placeholder

1.

Position of protein in relation to membrane bilayer (red represents periplasmic side while blue represents cytoplasmic layer) (2oau).

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Morph: 2oau to 2vv5.

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{Using the scene to the right showing the structure of E. coli McsS as well as the morph between the open and closed conformation, which side undergoes the most major conformational change.

Cytosolic
Periplasmic
→ Why might the smaller periplasmic side be the site of conformational shifting? What other functions might the cytoplasmic domain serve?

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

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→ 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?

[[

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[[

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[[

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[[

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