Why will the phi/psi angles of an amino acid in an alpha-helix be different from the...
Why will the phi/psi angles of an amino acid in an alpha-helix be different from the phi/psi angles of an amino acid in a beta-sheet? How are phi/psi angles possible fro Pro and for Gly different from those of other amino acids?
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Why will the phi/psi angles of an amino acid in an alpha-helix
be different from the...
A small generic section of the primary structure of an alpha helix is given below -amino...
A small generic section of the primary structure of an alpha helix is given below -amino acid1-amino acid2-amino acid3-amino acid4-amino acid5-amino acid-6-amino acid7- a.) which amino acid residue's backbone forms a hydrogen bond witht he backbone of the seventh(7th) residue? 6, 1, 3, 2, 5, OR 7? b.) which of the following peptide segments is most likely to be part of a stable alpha helix at physiological pH? a.) -Lys-Lys-Ala-Arg-Ser- b.) -Gly-Arg-Lys-His-Gly- c.) -Pro-Leu-Thr-Pro-Trp- d.) -Gly-Gly-Gly-Ala-Gly- e.) -Glu-Glu-Glu-Glu-Glu- f.) -Glu-Leu-Ala-Lys-Phe-...
3. What do the Phi (Q) and psi (y) angles represent? How do these angles differ...
3. What do the Phi (Q) and psi (y) angles represent? How do these angles differ between a-helix and B-sheet secondary structures?
Consider the Ramachandran Plot for polyglycine: Why is the phi = 0 and psi = 0...
Consider the Ramachandran Plot for polyglycine: Why is the phi = 0 and psi = 0 region not populated? Why are positive phi values allowed when they are not observed in other amino acids?
11.Which of the following mutations would most likely to disrupt the structure of an α-helix? Cys...
11.Which of the following mutations would most likely to disrupt the structure of an α-helix? Cys to Ala Lys to Arg Glu to Gly Val to Leu 12.Which amino acid combination is the most preferred to occupy positions 1 and 4 in an α-helix? Glu and Lys Phe and Pro Lys and Arg Asp and Glu 13.If each turn in the standard alpha helix extends 5.4 A and there are 3.6 amino acid residues per turn, how many amino acids...
Understand alpha helices and beta pleated sheets Question How is it possible for the a-helix to have amino acids with b...
Understand alpha helices and beta pleated sheets Question How is it possible for the a-helix to have amino acids with bulky side chains while the B-pleated sheets cannot? Select the correct answer below: O The R groups in the a-helix stabilize the structure, while they interfere with the hydrogen bonds in a B-pleated sheet. The R groups are contained inside the a-helix structure, while they interfere with the hydrogen bonds in a B- pleated sheet. O The R groups lie...
Question 11. Certain amino acids destabilize or prevent formation of alpha-helices. Which amino acid is more...
Question 11. Certain amino acids destabilize or prevent formation of alpha-helices. Which amino acid is more likely to be found in these structures based on its charge and R-group size? A. Glycine B. Proline C. A sequence of several Glutamate D. A sequence of several Lysine E. Alanine Question 12. Which of the following is least likely to result in protein denaturation? A) Altering net charge by changing pH B) Changing the salt concentration C) Disruption of weak interactions by...
There are four amino acid residues between each turn of an alpha helix, because O hydrogen...
There are four amino acid residues between each turn of an alpha helix, because O hydrogen bonding between the carbonyl and amine groups is more stable at this distance. O amino acid residues need a certain amount of distance between then during the turn. O the polar amino acids are more attractive to the peptide bond at this distance. O None of the choices are correct.
6. The following polypeptide (30 amino acids) contains a great deal of regular secondary structure. (10)...
6. The following polypeptide (30 amino acids) contains a great deal of regular secondary structure. (10) (15) (20) lys Lys Ala-Phe-Trp-Met-His- GIh-Thr-lle-Arg-Ser-Gly-Ala-Gly-Ser-Gly-Ala-Trp-Tyr-Pro-Val-Ala (30) Phe-Met-Leu-Val-Pro-Glu-Glu There are at least two regions where alpha helical structure is found. Indicate the beginning and ending residues of these regions. Any group or groups which break the alpha helical structure should not be considered part of the helix. Remember that it take four residues to give a turn of an alpha helix, so that is...
1.) Draw the structure of the amino acid Serine(ser), which has R=-CH2-OH. Label the alpha carbon. 2.) Draw the dipeptid...
1.) Draw the structure of the amino acid Serine(ser), which has R=-CH2-OH. Label the alpha carbon. 2.) Draw the dipeptide that forms between serine and alanine. The dipeptide sequence is Ser-Ala. Label the peptide bond. 3.) How many amino acids residues are in a polypeptide containing 6 peptide bonds? How many peptide bonds are in a tripeptide 4.) Sketch a alpha-helix and a beta-sheet as best as you can. Label each.
Understand alpha helices and beta pleated sheets Question Every helical turn in an a-helix has 3.6 amino acid residues....
Understand alpha helices and beta pleated sheets Question Every helical turn in an a-helix has 3.6 amino acid residues. Then, hydrogen bonds are formed between the oxygen atom in amino acid along the the carbonyl group in the first amino acid and the hydrogen atom in the amine group of the chain. Select the correct answer below: third second fourth fifth FEEDBACK MORE INSTRUCTION SUBMIT Content attribution
3. What do the Phi (Q) and psi (y) angles represent? How do these angles differ between a-helix and B-sheet secondary structures?
Consider the Ramachandran Plot for polyglycine: Why is the phi = 0 and psi = 0 region not populated? Why are positive phi values allowed when they are not observed in other amino acids?
Understand alpha helices and beta pleated sheets Question How is it possible for the a-helix to have amino acids with bulky side chains while the B-pleated sheets cannot? Select the correct answer below: O The R groups in the a-helix stabilize the structure, while they interfere with the hydrogen bonds in a B-pleated sheet. The R groups are contained inside the a-helix structure, while they interfere with the hydrogen bonds in a B- pleated sheet. O The R groups lie...
Question 11. Certain amino acids destabilize or prevent formation of alpha-helices. Which amino acid is more likely to be found in these structures based on its charge and R-group size? A. Glycine B. Proline C. A sequence of several Glutamate D. A sequence of several Lysine E. Alanine Question 12. Which of the following is least likely to result in protein denaturation? A) Altering net charge by changing pH B) Changing the salt concentration C) Disruption of weak interactions by...
There are four amino acid residues between each turn of an alpha helix, because O hydrogen bonding between the carbonyl and amine groups is more stable at this distance. O amino acid residues need a certain amount of distance between then during the turn. O the polar amino acids are more attractive to the peptide bond at this distance. O None of the choices are correct.
6. The following polypeptide (30 amino acids) contains a great deal of regular secondary structure. (10) (15) (20) lys Lys Ala-Phe-Trp-Met-His- GIh-Thr-lle-Arg-Ser-Gly-Ala-Gly-Ser-Gly-Ala-Trp-Tyr-Pro-Val-Ala (30) Phe-Met-Leu-Val-Pro-Glu-Glu There are at least two regions where alpha helical structure is found. Indicate the beginning and ending residues of these regions. Any group or groups which break the alpha helical structure should not be considered part of the helix. Remember that it take four residues to give a turn of an alpha helix, so that is...
Understand alpha helices and beta pleated sheets Question Every helical turn in an a-helix has 3.6 amino acid residues. Then, hydrogen bonds are formed between the oxygen atom in amino acid along the the carbonyl group in the first amino acid and the hydrogen atom in the amine group of the chain. Select the correct answer below: third second fourth fifth FEEDBACK MORE INSTRUCTION SUBMIT Content attribution
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