2. (6) Examine the two proteins labelled a) and b). Which of the two Ramachandran plots, c) or d) is morelikely to be derived from which protein? Explain how you determined this.(a)(b)(c)(d)✓ (degrees)✓ (degrees)+-18012060-60-120-180-180+18012060-120-180-1800(degrees)0(degrees)+180+180

Amino acids are backbone of proteins or polypeptide chains. When amino acids joined covalently…

Answered: 2. (6) Examine the two proteins…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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You are trying to determine the PTMs on your protein of interest, so you set up a mass spectrometry experiment. You get the following data. Starting sequence: PRTEINSKICKASSDER After Trypsin digest, you get the following major peptides and weights from MS: TEINSKICK/1167 Da ASSDER/664 Da a. Which of these peptides is modified? b. What is the modification?
33. Gel filtration chromatography shows that the molecular weight of a protein is 240,000 Daltons. However, when the protein was subjected to SDS-PAGE in the absence of ß- mercaptoethanol, two polypeptides (100,000 Daltons, 140,000 Daltons) were identified. Furthermore, when the protein was subjected to SDS-PAGE in the presence of ß- mercaptoethanol, three polypeptides (100,000 Daltons, 90,000 Daltons, and 50,000 Daltons) were identified. Which of the following statements is true of the protein? A. The protein is composed of three polypeptides. B. The three-dimensional structure of the protein is stabilized by both covalent and non- covalent bonds. C. Both A and B. D. Neither A nor B. 34. What is purpose of SDS in SDS-PAGE? E. To selectively bind the target protein F. To maintain buffer pH in the gel G. To cause the separation of proteins to be on the basis of molecular weight only H. To initiate polymerization of acrylamide to form gel
1a) In MALDI-TOF data, when performing peptide mass mapping search, the number of peptides and the sequence coverage decreases, but protien score increase. Explain b) As the same as part a, the peptide masses and the coverage remain the same, but the protien score increase, explain how this can happen.
please answer the full question
4. You're working on a structure of a protein and its folding. You think that the interaction between Asp123 and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29> Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29> Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein įs able to fold normally.…
1. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Gly-Trp-Phe-Met-Cys- What is observed when the protein sample is subjected to Millon’s test? Violet interface Red precipitate/solution Brown/black precipitate Yelllow product No observable result 2. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Tyr-Trp-Phe-Cys-Gly - What is observed when the protein sample is subjected to lead sulfide test? Violet interface Red precipitate/solution Brown/black precipitate Yelllow product No observable result
4) Researcher #1 and #2 in your lab each conducted a protein purification. They present you with the following data. The protein-of-interest is indicated by the red arrowhead, and the numbers on top indicate the purification step. Researcher #1 1 2 3 4 SDS-PAGE (Coomassie Stained) Researcher #2 1 2 3 4 5 6 Immunoblot a) Which researcher has more clearly demonstrated purification of the protein-of-interest? Justify your answer. b) What type of chromatography step did researcher #1 most likely conduct in going from step 2➜ 3 based on the gel? Justify your answer.
4)
I need to solve the following choices
For each of the following ( A & B ) provide the method of transfer and a brief explanation as to why the method would not take place under the conditions described . 1. Which method of DNA transfer between bacteria would not take place if the donor and recipient were separated by a filter with a pore size of 0.45 um or another physical barrier 2. Which method of transfer would be blocked by the presence of high concentrations of DNAase ( enzymes capable of degrading DNA ) ?

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