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My report on "Four Levels of Protein Structure"
My report on "Four Levels of Protein Structure"
Student name: khamiya Henry
Teacher name: wilsonda
School: Uuniversity of Southern Caribbean
Submission Time: 1/30/11 6:00 AM
Page 1 : http://mw2.concord.org/public/part2/proteinfolding/page1.cml
1. Use the Do It Yourself controls above to create a view that shows how the protein is folded. Use the text tool to label each end of the folded chain.
NOT ANSWERED.
2. Create a view that you think best shows the primary structure of parvalbumin. Use the text tool to explain why you chose this way of representing the primary structure.
(4:32:01 AM)
Page 2 : http://mw2.concord.org/public/part2/proteinfolding/page2.cml
1.
(4:52:02 AM)
2. Use the link above to open and explore the 20 rotatable 3D amino acids. Then select the "Sidechain" color scheme. The atoms that are colored gray are the same in every amino acid. What are they called?
(a) the sidechain atoms
(b) the backbone atoms
(c) the protein atoms
My answer is (b) (4:36:02 AM)
3. On the page of 3D amino acids, find glutamine and histidine. Use the different color schemes to select the true statement(s) below. (More than one statement may be true).
(a) they are both polar amino acids
(b) one is polar and the other is non-polar
(c) one of them is charged
(d) they are both non-polar
My answer is (a) (c) (4:41:25 AM)
Page 3 : http://mw2.concord.org/public/part2/proteinfolding/page3.cml
1. Take a snapshot of an alpha helix that shows how it folds.
(5:03:12 AM)
2. Take a snapshot of a beta sheet that shows how much space it occupies within the protein. Hint.
(5:04:48 AM)
Page 4 : http://mw2.concord.org/public/part2/proteinfolding/page4.cml
1. Hydrogen bonds stabilizing an alpha helix. Use the arrow tool to point out the hydrogen bonds.
(5:09:53 AM)
2. Hydrogen bonds stabilizing a beta sheet. Use the arrow tool to point out the hydrogen bonds.
(5:10:25 AM)
3. Hydrogen bonds stabilizing alpha helices and beta sheets form between the atoms of which part(s) of the amino acids involved?
(a) the side chains
(b) the side chains and backbone
(c) the backbone
My answer is (c) (5:11:36 AM)
4. Place a snapshot here that illustrates your answer to the previous question.
(5:12:48 AM)
Page 5 : http://mw2.concord.org/public/part2/proteinfolding/page5.cml
1. Is water a polar or non-polar molecule? Explain your answer by writing about the bonds in water.
NOT ANSWERED.
2. Which type of amino acid is hydrophobic?
(a) polar
(b) non-polar
(c) neither - they both don't attract water very well
(d) neither - they attract the water molecules equally
My answer is (b) (5:14:53 AM)
3. Which of the following correctly describe the interactions of the amino acids with water? (Check ALL that apply.)
(a) non-polar amino acids are repelled by water
(b) non-polar amino acids are weakly attracted to water
(c) water molecules are attracted to each other more than to non-polar amino acids
My answer is (b) (c) (5:15:41 AM)
4. Use your knowledge of positive and negative charge to explain why polar molecules attract each other better than non-polar molecules.
this because they are unlike negative attract positive... (5:54:50 AM)
5. Which solvent(s) leads to folding of the protein?
(a) both water and oil
(b) neither water nor oil
(c) water
(d) oil
My answer is (c) (5:19:31 AM)
6. Where do the amino acids with polar side chains end up when the protein chain folds?
(a) evenly throughout the folded protein
(b) mostly inside the folded protein
(c) mostly on the outside of the folded protein
My answer is (c) (5:19:46 AM)
Page 6 : http://mw2.concord.org/public/part2/proteinfolding/page6.cml
1. Show an interaction that stabilizes two alpha helices to each other. Use the annotation tool to label the type of interaction you are showing.
(5:26:07 AM)
2. Create a view that shows both the amino acids at the surface and those that fold into the inside the protein. Use the annotation tools to label the part that is more attracted to water.
(5:27:15 AM)
Page 7 : http://mw2.concord.org/public/part2/proteinfolding/page7.cml
1. On the left is a different small molecule than NAD. Why wouldn't this molecule bind to alcohol dehydrogenase in place of NAD? (Choose the BEST answer below).
(a) it is not the same as NAD
(b) it is smaller than NAD
(c) it is too large to fit in the NAD site
(d) it's the wrong shape, and will not form attractions with the site
My answer is (d) (5:30:10 AM)
2. What would you expect to happen to the function of proteins at very high temperatures?
(a) the functions would not be affected
(b) the proteins would not be able to function
(c) the functions would happen faster
My answer is (b) (5:32:15 AM)
3. Explain your answer to the previous question.
the protein structure is changed and the protein becomes denatured and cannot carry out it's original function. (5:33:18 AM)
Page 8 : http://mw2.concord.org/public/part2/proteinfolding/page8.cml
1. Does TNF have the quaternary level of structure? Make sure to try different color schemes on the model of TNF above.
(a) yes
(b) no
(c) It is impossible to tell.
My answer is (a) (5:48:42 AM)
2. Explain your answer to the previous question:
because it has three identical subunits... (5:49:08 AM)
Page 9 : http://mw2.concord.org/public/part2/proteinfolding/page9.cml
1. The "primary structure" of a protein refers to:
(a) the folds of the protein
(b) the alpha helix and beta sheet structures
(c) the sequence of amino acids in the protein
(d) the number of protein chains in a structure
My answer is (c) (5:56:13 AM)
2. What part of an amino acid has properties (shape, charge) that are different from other amino acids?
(a) the side chain
(b) the backbone atoms
(c) the secondary structure
(d) none of the above
My answer is (b) (5:56:31 AM)
3. The protein shown at right has folded in water. Which of the following statements about it is FALSE?
(a) amino acid 14 is most likely hydrophobic
(b) amino acid 17 is most likely polar
(c) amino acid 22 is most likely polar
(d) amino acid 20 is most likely hydrophilic
My answer is (c) (5:51:52 AM)
4. Which of the following do hydrogen bonds help to stabilize? (Check ALL that apply.)
(a) primary structure
(b) secondary structure
(c) tertiary structure
(d) quaternary structure
My answer is (b) (c) (d) (5:52:30 AM)
5. Select the two correct choices: A protein with quaternary structure...
(a) is made of two or more chains of amino acids
(b) is always composed of identical subunits
(c) is always composed of different subunits
(d) can be a mix of identical and different subunits
My answer is (a) (d) (5:52:47 AM)
6. Why do defects in protein folding cause disease?
this is because it changes the structure and also the function of the protein thus resulting in disease (5:53:44 AM)
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