added part a of the question for clarity
Homework Answers
Q1, a) Please find the answer as below image,
Q2, C, Base on the analysis of given helix
structure
i) The nuber of amino acid resudue per turn in the alpha helix is 3.6
ii) The per residue rise is 1.5 Å which results the rise per turn is 5.4 Å.
iii) The psi and phi values for the alpha helix is t30 degree and 140 degree respectively.
d) i)
The below image explain the antiparallel beta strand with the hydrogen bonding is highlighed in red colur.
ii) There are two residues per repeat unit which gives the beta-strand a 7 Angstrom..
The anti parallel beta strand length is 7 Angstrom..
iii) The psi and phi values for the antiparallel beta pleated sheet are
psi = = -139 degree
phi = +135 degree
Add Answer to:
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And please explain.
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6. (a) Show the arrangement of the groups on the a carbon of the naturally occurring amino acids (draw out the stereocentre). (b) What is the significance of chirality in the biological world? 7. (a) Sh (a) Show the repeating unit of the polypeptide chain in a protein and indicate the peptide bond. (b) What are the following structures of a protein (i) primary, (ii) secondary, (iii) tertiary and (iv) quaternary. 1. Polypeptides are the natural polymer of the naturally...
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...
What happens when a primary structure forms a secondary structure? Match the words in the left column to the appropriate blanks in the sentences on the right. Make certain each sentence is complete before submitting your answer. Terms may be used once, more than once, or not at all. Reset Help carboxylic acid a helix When atoms in the backbone of a protein or peptide form within a single or between chains, a secondary structure results. The two most common...
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And please explain.
1. Read both parts A and B of question 1 before you answer either one. Draw a peptide backbone that extends for three amino acids. Label the psi, phi and omega angles, showing the direction of rotation. Indicate resonance. Draw the structure with the more likely cis or trans conformation. Indicate side chains with the letters R1, R2 and R3. A. B. Draw a second peptide below the one...
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