After completing the "Secondary structure" part of the Structure
section you will: |
In this section you can look at, and analyze some small, nearly perfect parts of molecules with a regular secondary structure.
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Figure 54. Load the file HELIX.pdb in Yasara. This is obviously not a real protein, but something we made up to make it easy for you to get used to looking at protein structures. |
Question 60: Describe the distribution in space (relative to the helix) of the side chains of the hydrophobic and hydrophilic residues.
AnswerQuestion 61: Describe the hydrogen bonding of the backbone atoms of the glutamic acid. Do the same for two other residues in the middle of the helix. Do you see a pattern emerge?
AnswerQuestion 62: Although this helix is energetically already rather favourable (compared to the unfolded form), it is not yet perfect. How can you improve the stability by changing its sequence?
Answer
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Figure 55. Load the file BETA1.pdb in yasara. This is obviously not a real protein, but someting we made up to make it easy for you to get used to looking at protein structures. |
Question 63:
Load the file BETA1.pdb in yasara.
Draw the 2D-projection of the backbones of the two strands. Include the hydrogenbonds
as dashed lines.
Question 64: Describe the hydrogen bonding pattern for the backbone of Phe-10.
AnswerQuestion 65: And now, without clicking in yasara, describe the hydrogen bonding pattern of Arg-9.
AnswerQuestion 66: Describe the spatial distribution (i.e. the distribution in three dimensions) of the side chains of the hydrophobic and hydrophilic residues. Do you see systematic effects in this distribution?
Answer
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Figure 56. Load the file BETA2.pdb in yasara. This, again, is not a real protein, but something we made up. |
Question 67: Draw the 2D-projection of the backbones of the two strands. Include the hydrogenbonds as dashed lines.
Answer
Question 68: Describe the hydrogen bonding pattern of Thr-3.
Answer
Question 69: Describe the hydrogen bonding pattern of Phe-4.
Answer
Question 70: Describe the spatial distribution in three dimensions of hydrophobic and hydrophilic residues.
Answer