proteins. Which of the following will tell you whether a protein would be found in the lumen of the ER?A. You run a hydropathy plot an look for hydrophobic peaks that span 20-30 amino acidsB. You isolate microsomes and see whether the proteins are inserted into the membrane of the microsomeC. You run a hydropathy plot an look for a lack of hydrophobic peaks that span 20-30 amino acidsO D. You do in vitro translation of each protein in the presence or absence of microsomes and look to see whether there is a size change in the presenceof microsomes.

An eukaryotic cell is heavily compartmentalized for each specific function. Eukaryotic cell is…

Answered: proteins. Which of the following will…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter30: Protein Synthesis

Section: Chapter Questions

Problem 7P

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Affinity chromatography You have created a fusion protein tagged with Glutathione-S-Transferase (GST). Your lab mate tells you that the affinity columns for this type of tagged protein are very similar to that of Histadine tagged proteins. Using the following elements set up a purification column and construct a protocol for an affinity purification using this tag. A large amount of glutathione is usually used to elute the tagged protein off the column. How might this work?
Which model (2D topology or trRosetta) is likely a better representation of the actual protein AlaE, why?
Purification of a new unknown protein that you isolated from tissue and Assume that you have reached the following data during the characterization; Gel filtration: Gel filtration in protein native conformation When chromatographed, it has a molecular weight of 240000 daltons (240 kDa) is detected to be around. Gel filtration: The same protein is first denatured with 6 M guanidinium hydrochloride subjected to gel filtration chromatography again under denatured conditions. is retained, and the only column from the column with a molecular weight of about 60000 daltons (60 kDa) a protein is obtained. SDS-PAGE: Protein finally SDS-PAGE in the presence of beta-mercaptoethanol (Sodium dodecyl-sulphate polyacrylamide gel electrophoresis) analysis being held. As a result of SDS-PAGE analysis, their weight in the gel is approximately 40000 daltons. Two protein bands corresponding to (40 kDa) and 20000 daltons (20 kDa) is observed. In the light of these findings, the quaternary/quaternary…
Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
True or false?: The CTD is responsible for mRNA-processing steps that are specific for mRNA and not for other forms of RNA. Explain why you chose true or false.
Plz choose all correct option and Do explain. Which of the following descriptions about tandem affinity purification is not correct? a.The interaction between calmodulin-binding peptides and calmodulin beads can be broken by adding EDT b.In the first round of elution, TEV protease cleaves the cleavage site on the TAP-fused target protein. c.It enables the purification of protein complexes composed of multiple protein components. d.It is possible to perform two rounds of purification using a single TAP tag. e.The protein A tag binds to beads that have lgG attached to them.
Help? Please explain salting out in protein purification.
High salt concentrations tend to cause protein aggregation. Suggest a way to identify proteins normally expressed in particular bacterial species that can retain their solubility despite high salt conditions.
DO NOT COPY OLDER ANSWERS! AND SHOW FULL WORK! I have a mixture of 4 proteins, whose sequences are shown below (note that each protein is a 100-repeat of the sequence shown). Protein A: (Gly-Ala-Lys-Val-Ile-Phe-Glu-Val-Asn-Gly) Protein B: (Ala-Ala-Lys-Arg-Ile-His-Glu-Ala-Asn-Lys) Protein C: (Glu-Val-His-Asp-Ala-Asp-Glu-Val-Asn-Asp) Protein D: (Ala-Lys-Arg-Phe-Trp-Phe-Gly-Ile-Ala-Gly) 1) Which protein/s are MOST LIKELY to precipitate out at a pH of 3.5? a) A b) B c) C d) D e) B & C f) A & D g) None of them h) Cannot be determined.
Simple problem-solving: Imagine you did a Bradford assay, and measured the absorbance of a set of protein standards and two unknowns. You repeated each measurement three times, and got the following readings in the table below. Concentration (micrograms/ml) A595 - trial 1 A595- trial 2 A595- trial 2 average A595 A595 of sample minus A595 of blank 0 1.501 1.446 1.447 1.465 0 2 1.624 1.558 1.559 1.580 0.115 5 1.731 1.749 1.712 1.731 0.266 10 1.901 1.838 1.892 1.877 0.412 15 2.161 2.108 2.228 2.166 0.701 18 2.231 2.277 2.319 2.276 0.811 unknown 1 - D1 1.717 1.713 1.644 1.691 0.226 unknown 2 - D1 1.668 1.649 1.656 1.658 0.193 concentration of unknown 1 concentration of unknown 2 Calculate the concentration of the unknowns and answer the following question: Did you need to do any manipulations before applying the…
Answer for each 1, 2, 3, 4 and 5 labelled in the attached image: a)What is this molecule? b)What superfamily does it belong to? c)Which number points to the peptide binding domain? Thank you!
Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. Extreme temperatures and pH can cause permanent disruption of the protein primary structure(s) of enzymes that leads to loss of active site shape, loss of binding efficiency and activity.

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