Question 17 Question Completion Status30313233341 2712131416171011QUESTION 17The titration curve shown here is most likely that ofOH ulvO alanineO glycineO histidineO phenylalanineO leucineQUESTION 18Protein regulation often requires phosphorylation of hydroxyl groups. Which of the following amino acids in a protein is a potential site for phosphorylation?O methionineO cysteineO asparagineO tyrosineQUESTION 19ey are often used as buffers. In this titration curve of glycine which is the best pH region(s) I, II, IV for optimal buffering capacity of glycine? Clue: there is aClick Save All Answers to save all answers.Save All Answers77 6el SaypedS SptMyCur

A titration of amino acids is a process in which base added gradually to neutralize the acids, the…

Answered: Question Completion Status 30 31 32 33…

Biochemistry

9th Edition

ISBN:9781305961135

Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Chapter3: Amino Acids And Peptides

Section: Chapter Questions

Problem 54RE: THOUGHT QUESTION Imagine we identify a gene that is directly responsible for the effects of...

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QUESTION NO. 1Targeting a protein to be degraded within proteasomes usually requires ubiquitin. In the function of ubiquitin all of the following are true except: A. ATP is required for activation of ubiquicin. B. a peptide bond forms between the carboxyl terminal of ubiquitin and an ε-amino group of a lysine . C. linkage of a protein to ubiquitin does not always mark it for degradation. D. the N-terminal amino acid is one determinant of selection for degradation. E. ATP is required by the enzyme that transfers the ubiquitin to the protein to be degraded QUESTION NO. 2Much of procollagen formation occurs in the endoplasmic reticulum and Golgi apparatus which requires signal peptide. All of the following statements about targeting a protein for the ER are true except. A. signal peptide usually has a positively charged N-terminus and a stretch of hydrophobic amino acids. B. signal peptide emerging from a free ribosome binds signal recognition…
Question: A decapeptide composed of ser, ala, IIe. his, trp, phe was treated with 1-flouro- 2,4-dinitrobenzene. It gave a DNP-his on the N terminal and free trp when treated with carboxypeptidase. Upon partial hydrolysis of the peptide, the following fragments were obtained. a. his-lle-phe-ala c. his-ala-phe e. ser-lle-his b. ala-phe-trp d. phe-ala-ser Give the amino acid sequence of the above decapeptide.
student question 1. How do both Hemoglobin and S-adenosylmethionine synthetase form hydrophobic pockets? explain in detail. 2. how does the structure of S-adenosylmethionine synthetase make it resistant to heat denaturation and why, explain in detail
510. Trypsin cleaves proteins after lysine and arginine residues. Trypsin itself has 13 lysine and 2 arginine residues in its primary structure. Why does trypsin not cleave itself into 16 smaller peptides?
Question 1 options: The specificity pocket of the serine protease chymotrypsin, which interacts with Tyr and Phe-containing peptide sequences, contains a Ser residue. A research group is trying to modify chymotrypsin such that it has a low KM with Trp-containing peptides. Enter the name or abbreviation of an amino acid that the Ser could be mutated to that would likely have the desired effect. (Hint: look at the diagrams of the specificity pockets shown in the course slides, and consider how the Ser would need to change to account for the difference between Tyr/Phe and Trp.)
Question:- Based on the figure below, predict what peptide bond could be the substrate of each protease(The bond marked in blue is where hydrolysis occurs, choose 2 peptides per protease type) Chymotrypsin:_________ Trypsin:_________ Elastase:_________ 1. SR−SG 2. SF−SG 3. SK−SG 4. SA−SG 5. SV−SG 6. SM−SG
Time remaining: 00:08:55 Chemistry Consider a peptide with the following amino acid sequence: H2N-ASENHLDGCPYTKSRG-COOH Analyze the predominate protonation state and thus dominate charge (+1, 0, -1) of the residues in this peptide at pH 3, 6, and 10 by filling in the table below, identifying the relevant pKa appropriate for each residue. (Note that choice of pKa and its. application will be graded independently; e.g., if you can choose the wrong pKa but apply it correctly, you will lose points only for the pKa.) AA Residue pKa Charge pH 3 Charge pH 6 Charge pH 10 A S E N H L D G C P Y T K S R G
Can Please Help Me: Bio- Chemistry 60 minutes only the given time. Wish you could help me. I will give UPVOTE and GOOD FEEDBACK. QUESTION/// Diisopropyl fluorophosphate (DFP) inhibit acetylcholinesterase activity by reacting covalently to a serine residue found within the active site of the enzyme. The physiological effect of this inactivation is interference with neurotransmitter inactivation at the synapses of nerves, resulting in the constant propagation of nerve impulses, which can lead to death. What type of inhibitor is DFP? Explain. ///QUESTION
Question 11. // Hint: Isoelectric focusing separates proteins based on their pI values, and can separate proteins that only differ by a net charge of ±1.±1. Recall that an amino acid residue with a negatively charged R group has a relatively low isoelectric point (pI) where it has zero net charge. Likewise, an amino acid residue with a positively charged R group has a relatively high isoelectric point (pI) where it has zero net charge. Order from Low pH to High pH
Question for protein crystallography- 1. While performing a routine protein crystallization screening, you observe that one of your well drops has doubled in size compared to the remaining wells. Note: the drop in question was set up by taking 1 µL of the protein solution (10 mg/mL LDH in 20 mM TRIS pH 7.5, 0.5 M NaCl and 10% PEG 4000K) and adding it to 1 µL of the crystallization solution (10% PEG 4000K, 50 mM NaCl and 20 mM TRIS pH 8.0). Why did this drop grow larger in size compared to when you initially set it up?
Enzyme: Crystal Structure of Wild-Type Human Phosphoglucomutase-1 (PGM1) the description of the mechanism of how this enzyme is regulated (e.g., depending on the enzyme, the mechanism could range from being solely dependent on gene regulation to protein structure-based mechanism).
Situational task: As a result of intoxication, enzymes that provide splicing are not synthesized in liver cells. What is the reason for stopping protein biosynthesis in this case? Justify the answer

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Question Completion Status 30 31 32 33 34 12 13 14 16 17 1 2 10 7 11 QUESTION 17 The titration curve shown here is most likely that of Oquiv O alanine O glycine O histidine O phenylalanine leucine