Download Protein Folding Questions only

Survey
yes no Was this document useful for you?
   Thank you for your participation!

* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project

Document related concepts

Structural alignment wikipedia , lookup

Implicit solvation wikipedia , lookup

Rosetta@home wikipedia , lookup

Protein design wikipedia , lookup

Circular dichroism wikipedia , lookup

Bimolecular fluorescence complementation wikipedia , lookup

List of types of proteins wikipedia , lookup

Homology modeling wikipedia , lookup

Protein domain wikipedia , lookup

Protein moonlighting wikipedia , lookup

Proteomics wikipedia , lookup

Protein purification wikipedia , lookup

Protein folding wikipedia , lookup

Protein wikipedia , lookup

Western blot wikipedia , lookup

Protein mass spectrometry wikipedia , lookup

Alpha helix wikipedia , lookup

Intrinsically disordered proteins wikipedia , lookup

Protein–protein interaction wikipedia , lookup

Cyclol wikipedia , lookup

Nuclear magnetic resonance spectroscopy of proteins wikipedia , lookup

Protein structure prediction wikipedia , lookup

Transcript
The Protein Folding Challenge – Answer these questions in your Lab Notebook
Amino acids – the building blocks of proteins
1.
Do you see similarities or patterns in the sidechains? Explain what you observed:
- Hydrophobic sidechains are composed primarily of __________________ atoms.
- Acidic sidechains contain two ______________ atoms. This is called a
___________________functional group.
- Basic sidechains contain __________________ atoms. This is called an __________________
functional group.
- Hydrophilic sidechains have various combinations of ____________. An exception to this observation is:
Folding a 15 amino acid protein
1. Predictions: From your experience with oil and water, which sidechains might position themselves on
the interior of a protein, where they are shielded from water? Why?
- Which sidechains might be attracted to each other? Why?
- Would the final shape of a protein be a high energy state or a low energy state for all of the atoms in
the structure? Why?
2. Which part of the model represents the backbone of the protein?
a. What do the metal clips represent?
3. What is the 15 amino acid sequence that you chose?
4. Sketch the Tertiary Structure of your protein or insert a photograph of it.
5. Why should Methionine be next to the Blue End Cap?
6. What happened as you continued to fold your protein and applied each new chemical property to your
protein?
- Were you able to fold your protein, so that all of the chemical properties were in effect at the same
time? If not, do you have any ideas why you weren’t able to fold your protein in a way that allowed all
of the chemical properties to be in effect simultaneously?
1
7. Did your protein look like the proteins other students folded? Explain.
8. How many different polypeptides, 15 amino acid long, could you make given an unlimited number of
each of the 20 amino acids?
9. Most real proteins are actually in the range of 300 amino acids long. How many different possible
proteins, 300 amino acids in length, could exist?
10. How many different proteins are found in the human body? (Another way to ask this question is - How
many different genes are there in the human genome?) If you need to, look this up on the internet and
provide the reliable source that you chose to use.
11. Assuming that all human proteins are 300 amino acids long, what fraction of the total number of
possible human proteins is actually found in the human body?
12. Why do you think there are fewer actual proteins than possible ones?
2