6) Proteins can be modified by phosphorylation, which adds aphosphate group to the hydroxyl group of serine, threonine, ortyrosine residues. The R-group for phosphoserine is shown at right.A) The image below is an Isoelectric focusing strip that shows theunphosphorylated protein-of-interest (in blue). To which side of theunphosphorylated protein would you expect to see the phosphorylatedprotein? (Draw an arrow to indicate direction).Briefly justify your answer.un-phosphorylatable:Low pHJustify:B) To study the effects of phosphorylation, researchers often mutate a Ser/Thr toappear as though it is always phosphorylated or never phosphorylated at a particularsite. What amino acid substitution should you use to preserve similar dimensions asSer (or Thr) but make the side chain appear to be:constitutively (always) phosphorylated:Justify:Ser or Thr →OO=P-OOICH₂Ser or Thr➜PhosphoserineHigh pH

Protein modification - Major types of proteins modifications are phosphorylation, acetylation and…

Answered: 6) Proteins can be modified by…

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 15QP

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Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide. I don't understand how the order of amino acids in Step 2 was arranged. Please explain. Thank you.
In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-Ser-Gln-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys-The hydrophobic residues in this sequence are presented in boldface type.Suggest a possible reason for the periodicity in their spacing.
Considering the chemical characteristics of the amino acids valine and glutamic acid (see Figure 5.14), propose a possible explanation for the dramatic effect on protein function that occurs when valine is substituted for glutamic acid.
What amino acid residue of phosphoglucomutase is able to transfer the phosphoryl group to glucose 1-phosphate? A. phosphorylated serine residue B. acetylated lysine residue C. phosphorylated tyrosine residue D. phosphorylated lysine residue E. acetylated serine residue
Here is a putative peptide sequence (position number on top of residues): 1 2 3 4 5 6 7 8 9 10 11 12 13 NH2- G C G N V T H N Q C V L S -COOH If expressed in a eukaryotic cell (please mark your answer in the blank space): Position(s) ___ could be N-glycosylated Position(s) ___ could be modified with myristic acid and the bond formed would be a ______________ Position(s) ______and _____ could be modified with palmiti c acid and the bond formed would be a ______________ Positio n(s) ________ could be a segment of a lipid-linked protein with a farnesyl anchor and the bond formed would be a ______________ Position(s) ________ could be a segment of an O-glycosylated protein Position(s) ________ could be modified with a glycosylphosphatidylinositol (GPI) anchor Position(s) ________ could be phosphorylated
What amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine? In relation to the amino acid in the specificity pocket, which peptide bond is cleaved; C terminal or N terminal? What is this bond’s proximity to the serine in the active site?
Consider a globular protein that contains an alpha-helix within it: a) Suppose there is a ligand binding pocket in this alpha-helix that contains residues of Leu (2), Phe (5), Gly (6), Ala (18), Tyr (22), Tyr (28), Gly (30), Cys (45), His (48) and Asp (49). What does this tell us about the likely nature or characteristics of a potential binding ligand? I said tha because 6/10 of the amino acids in this binding pocket are non-polar, that the ligand is also non-polar, but I think the question needs more description about the ligand. b) Briefly describe the driving forces and energetics behind folding of globular proteins (use terms like ΔH, ΔS, and ΔG) I said that H = -, S = +, G = - Folding driving force would likely be entropy change from non-polar residues interacting with a solvent (ex: water). Hence, non-polar residues would be buried in the globular protein structure from folding, causing entropy to increase for any liberated solvent molecules. Not 100% sure if this is correct,…
Draw a fractional binding curve for trimeric protien that has a binding site on each subunit. Moreover, the protein has a preferred low affinity conformation.
Imagine that a mutation has been discovered in the HBA1 gene, where amino acid residue # 1 in the alpha subunit is changed from valine to lysine. The structure of these two amino acids is shown below. How would this mutation affect the mobility of HbA in the gel?a) HbA with this mutation would have the same mobility as normal HbAb) HbA with this mutation would have the same mobility as HbSc) HbA with this mutation would have a faster mobility than normal HbA O d) HbA with this mutation would have a mobility somewhere in between HbS and normal HbA
a) At what pH will you try to bind lysozyme to a cation exchanger? b) Is it possible to perform this binding even at a different pH than the one you mentioned in section a? Explain your answer. c) Is it possible to bind lysozyme to an anion exchanger as well? If so, at what pH?
A lysine is on the surface of a protein, near an aspartate. How does the aspartate alter the pKa of the lysine?
For each of the following sequences determine if they will most likely form an amphipathic α helix, amphipathic β sheet, turn/loop or not an amphipathic structure. A) Lys-Gln-Asn-Glu-Pro-Arg-Ala-Asn-Glu B) Lys-Ser-Thr-Asn-Glu-Gln-Asn-Ser-Arg C) Gln-Ile-Thr-Phe-Thr-Leu-Gln-Val-Ser D) Asn-Leu-Ala-Asp-Ser-Phe-Arg-Gln-Ile

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