Why do helices make better folding nuclei when compared to beta sheets?
This is due to the fact that when helices forms hydrogen bonding also tends to takes place within the helix itself and thereby stabilizing it.
Beta sheets are less stable because of energy barrier that arises between folded and non folded state.
Thus due to this reason helices makes better folding nuclei in comparison to that of beta sheets.
Hope this helps you
Why do helices make better folding nuclei when compared to beta sheets?
1) Indicate why alpha helices and beta sheets help "bury" hydrophobic amino acids in the interior of a folded polypeptide in an aqueous environment. 2) Explain what is meant by the statement "Protein folding is driven by hydrophobic interactions" and under what conditions this is true.
Classify each phrase as a description of alpha helices, beta sheets, beta turns, or all. a Helices B Sheets B Turns All Answer Bank successive R groups point in opposite directions all - NH groups point in the same direction contains - NH hydrogen-bonded to C=0 first residue hydrogen-bonded to fifth residue that is, residue n is H-bonded to residue n+4) first residue hydrogen-bonded to fourth residue (that is, residue n is H-bonded to residue n+3)
I have a few questions about alpha-helices and beta-sheets. 1)Is there a tendency for the polypeptide chains to become one form of the secondary structure over the other? 2)Are there specific advantages and/or disadvantages to being in the alpha-helix or beta-sheet state? 3)What causes the polypeptide chain to fold in a particular way?
Understand alpha helices and beta pleated sheets Question Which amino acid from the following list best fits the B-pleated sheet? Select the correct answer below: tryptophan alanine arginine lysine FEEDBACK MORE INSTRUCTION SUBMIT Content attribution
Why is proline unfavorable for the formation of alpha-helices? The sidechain is too flexible for a turn. The sidechain is too rigid to bend into a turn. It is better suited for beta-turns O The sidechain is incapable of hydrogen bonding
Understand alpha helices and beta pleated sheets Question Which of the following statements is not true about R groups in B-pleated sheet? a. The R groups of the peptide chain point outside. b. The R groups are attached to the carbons and extend above and below the folds of the pleat. c. The amino acids tend to have smaller R groups. Select the correct answer below: a and b a and c b and c only a FEEDBACK MORE INSTRUCTION...
Part A Which is not true about beta-sheets? Antiparallel sheets provide better hydrogen bonding than parallel sheets Antiparallel is when two peptide strands run in opposite directions The sheets are pleated The side chain of the residues are side-by-side (planar) to the peptide backbone
Part A Which is not true about beta-sheets? O Antiparallel sheets provide better hydrogen bonding than parallel sheets O Antiparallel is when two peptide strands run in opposite directions. O The sheets are pleated The side chain of the residues are side-byside (planar) to the peptide backbone. Submit Request Answer
Understand why formation of α-helices and β-sheets is energetically favorable. Just need background info/summary.
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