Bichemistry questions Can somebody help me answer the questions above, and expla
ID: 54403 • Letter: B
Question
Bichemistry questions
Can somebody help me answer the questions above, and explain how did you do it so I can understand?
For question 62, 64, 65, use the tripeptide VDF to answer the question.
The alphabets represent the amino acids. For example, V stands for Valine, D stands for Aspartate, I stands for Isoleucine, S stands for Serine, etc.
you can look at the structure of the amino acids here:
For the next 9 questions, consider the following fragments obtained from cutting a 20 residue pepide 1) FDED 2) LAEAPGMG 3) WAH 4) WEDTML 29) Based on the cleavage pattern, the peptide was most lkely cut with a. Pepsin b. Chymotrypsin C. Asp-N-protease d. Endoproteinase Lys C e. None of the above 30) Which of the tollowing statement is true: a. None of the below b. You can identify the C-terminus c. You can identify the N-terminus d. Both a and b e. Chymotrypsin would produce the same fragment pattern 31) What type of lon-exchange column and peptide order could be used to separafe above fragments at pH 7.07 31) What type of ion-exchange column and peptide order could be used to separate above fragments at pH 7.0? Anion exchanger produces a peptide order of b. a. 1, 4, 2, 3 3, 4, 1, 2 3, 1, 4, 2 2, 1, 4, 3 3,2, 4, 1 Cation exchanger produces a peptide order ot C. Anion exchanger produces a peptde order of d. Cation exchanger produes a peptde order of e. Anion exchanger produces a peptide order ot 32) Can the peptide sequence be determined from the above information? (select most correct answer) a. Yes b. No, only need to identify the carboxyl terminal residue to determine sequence order C. No, only need to idenily the amino terminal residue to determine sequence order d. No, need to recut with peptide again with cyanogen bromide and resequence e. No, need to recut the peptide again with trypsin and reseqeunce 33) At pH = 1, which peptide a neutral charge? 34) At pH = 13, the peptide with the lowest negative charge is 35) what is the best explanation as to why peptide #1 would not take on an alpha helical conformation? e) none of them d) 4 e) they all have the same charge nation 9)3 negall 4 a. too short contains an amino acid restricted in phi,psi space sequence favors sheet formation contains a amino acid branched at the beta carbon none of the above d. e. Use the following list to answer the next 2 questions about the peptides at the top of the page. b) 2, 4, 1, 3 c) 1, 2,3,4 d) 4, 3, 2,1 e) none of these a) 3, 1, 4, 2 36) Using a size exclusion column, what order would you get of the column 36) Using a size exclusion column, what order would you get off the column (assuming the molecular weight cutoff of the column material was large enough to handle all the peptides). 37) Using SDS-PAGE, what would the order be on the stained gel from bottom to top.nExplanation / Answer
62. The correct answer is option a.
The tripeptide VDF has 3 chiral centres.
64. The correct answer is option e.
phi () is the N(i-1),C(i),Ca(i),N(i) torsion angle.
65. The correct answer is option e.
psi () is the C(i),Ca(i),N(i),C(i+1) torsion angle.
67. The correct answer is option e.
The interaction between 2" and 3" structures are similar to hydrophobic interactions with water.
68. The correct answer is option b.
For most amino acids the +phi, - psi quadrant is most disallowable.
69. The correct answer is option d.
Residues in helical conformation are in -phi, +psi quadrant.(Though helices are also found in -psi,-phi and +psi, +phi qudarants.)
70. The correct answer is option d.
Residues in sheet conformation are in -phi, +psi quadrant.
71. The correct answer is option a.
Left handed helices are found in +phi,+psi quadrant.
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