Solution:
Option A, left handedness is not generally observed in α-helices.
The α-helix is a common secondary structure exhibited by proteins along with beta sheets. Generally they are of right handed-helix.The hydrogen bond is formed between the CO group of one amino acid with the NH group of the amino acid that is situated four residues ahead in the sequence. The α-helix is tightly packed and the amino-acid side-chains are pointes towards the outside of the helix. Also it possess cylindrical shape. Each residue is related to the next one by a rise of 1.5 Å along the helix axis and a rotation of 100 degrees, that gives 3.6 amino acid residues per turn of helix.
QUESTION 20 Which of the following is not a feature commonly observed in a helices? A....
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
Explain why α-helices are most commonly observed in
transmembrane protein sequences when the distance from one side of
a membrane to the other can be spanned by significantly fewer amino
acids in a β-strand conformation.
Match the items in the left column to the appropriate blanks in
the sentences on the right.
prevents within a The structure of an a-helix promotes stretch of amino acids, and at the same time contiguous interactions with other important molecules involved in in the...
Explain why α-helices are most commonly observed in
transmembrane protein sequences when the distance from one side of
a membrane to the other can be spanned by significantly fewer amino
acids in a β-strand conformation.
Match the items in the left column to the appropriate blanks in
the sentences on the right.
noncontiguous The structure of an a-helix promotes within a stretch of amino acids, contiguous and at the same time interactions with other important molecules involved in in the...
QUESTION 21 Which of the following is not a feature commonly observed in ß sheets? O A parallel regions OB. extended polypeptide backbone OC.coiled-coil patterns O D. antiparallel regions QUESTION 22
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...
Multiple Choice Question, Please Pick the Correct Option for
Each Question (Only one option is correct per question)
Part A The amino acid that destabilizes alpha-helical structures and is usually found at the ends of alpha helices is O Alanine Glycine Asparagine O Glutamate PART B Proline is NOT often found in a-helices of proteins because it O Lacks a hydrogen atom on its amide nitrogen O Interacts with adjacent amino acids Has a very bulky side chain O Has...
Understand alpha helices and beta pleated sheets Question The coiling of an a-helix is maintained in position by which of the following bonds? Select the correct answer below: O hydrogen bonds between the oxygen atom in the carbonyl group in one amino acid and the hydrogen atom of the hydroxyl group in an R-group of another amino acid that is four amino acids farther along the chain O hydrogen bonds between the oxygen atom in the carbonyl group in one...
Which of the following is true about quaternary structures of proteins? a. It is the three-dimensional shape of a protein consisting of a single peptide chain. b. It is the three-dimensional shape of a protein consisting of a multiple peptide chains. c. It is the order of amino acids in the peptide chain. d. It is the number of alpha helices in the peptide chain.
Understand alpha helices and beta pleated sheets Question The coiling of an a-helix is maintained in position by which of the following bonds? Select the correct answer below: hydrogen bonds between the oxygen atom in the carbonyl group in one amino acid and the hydrogen atom of the hydroxyl group in an R-group of another amino acid that is four amino acids farther along the chain O hydrogen bonds between the oxygen atom in the carbonyl group in one amino...
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...