What would the order of migration be (bottom to top in the gel) in a SDS-PAGE for thefollowing proteins? Concanavalin A (ConA) (a homotetramer of 106 kDa), lysozyme (amonomer of 14.3 kDa) & horse liver alcohol dehydrogenase (ADH) (a homodimer of 80kDa).a. ADH, ConA, lysozymeb. ConA, ADH, lysozymec. Lysozyme, ADH, ConAOd. Lysozyme, ConA, ADH

Introduction: Sodium dodecyl sulfate-polyacrylamide electrophoresis (SDS-PAGE) is an analytical…

Answered: What would the order of migration be…

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 20QP: If an extra nucleotide is inserted in the first exon of the beta globin gene, what effect will it...

See similar textbooks

Similar questions

a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Draw the pathway leading to the production of protein E.
A recent genome sequencing project for the bacterium Burkholderia mallei has identified a new protein with high similarity to the lysylphosphatidylglycerol flippase enzyme. A short section of the new protein sequence is shown below. TVEVNAPGDVQKALSELQQINDGRLDIRI (a) Are any reverse turns likely to be present? Explain your answer. (b) Are any beta-strands likely to be present? Explain your answer. (c) Are any alpha helices likely to be present? Explain your answer. (d) Is any supersecondary structure likely to be present? Explain your answer. (e) Identify two residues that are likely to be buried in the core of the folded protein. Explain your answer. (f) Identify two residues that are likely to be hydrogen bonded to each other. Explain your answer.
Electrophoresis is performed at PH 6.8 on a mixture of mutated hemoglobin that differ from normal haemoglobin (Hb) only by the substitution of one amino acid- Hb X: Val replaced par Glu - Hb Y: Asp replaced by Leu - Hb Z: Glu replaced by Lys What will be the order of migration between cathode and anode of these mutated Hb compared to normal Hb? Justify your answer.
This molecule forms a dimer via pi interactions, resulting to effective molecular stacking. If the molecule can inhibit toxic effects at 0.5mM against gastric carcinoma cells, does it mean that the dimer of this nucleoside analogue will exhibit an IC50 of about 0.25mM?
Imagine a globular protein with a histidine that is involved in a salt bridge to an aspartic acid, in an internal (hydrophobic) region of the protein. What would happen to the pKa of that histidine R group if the protein was mutated, and the aspartic acid was replaced with an alanine? (i.e., would the pKa increase, decrease, or stay the same?). Assume that the location of the histidine stays the same. Explain your answer clearly
Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individual’s cell in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individual’s cells are given in the following table. A plus sign means that the protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. a) If an individual who is homozygous for the mutation found in individual 2 and heterozygous for the mutation found in individual 4 mates with an individual who is homozygous for the mutation found in individual 4 and heterozygous for the mutation found in individual 2, what could the…
Take a look at the multiple-sequence alignment shown ofthe globin polypeptides, focusing on amino acids 101 to 148.A. Which of these amino acids are likely to be most important forglobin structure and function? Explain why.B. Which are likely to be least important?
How many copies of a protein need to be presentin a cell in order for it to be visible as a band on an SDSgel? Assume that you can load 100 μg of cell extract ontoa gel and that you can detect 10 ng in a single band by sil-ver staining the gel. The concentration of protein in cellsis about 200 mg/mL, and a typical mammalian cell has avolume of about 1000 μm3 and a typical bacterium a vol-ume of about 1 μm3. Given these parameters, calculatethe number of copies of a 120-kd protein that would needto be present in a mammalian cell and in a bacterium inorder to give a detectable band on a gel. You might try anorder-of-magnitude guess before you make the calcula-tions.
If this molecule can inhibit toxic effects at 0.5mM against gastric carcinoma cells, does it mean that the dimer of this nucleoside analogue will exhibit an IC50 of about 0.25mM?
During SDS-PAGE, glycoproteins migrate as relatively diffuse bands, whereas nonglycosylated proteins typically migrate as narrow, well-defined bands. Explain the reason for this difference in electrophoretic behavior.
If a new isolated protein called STICKY and this STICKY protein contains a bHLH domain. Now, how we predict the function of STICKY and the rationale for the importance of these domains in the STICKY function?
. Disulfide bonds have been shown to stabilize proteins (i.e., make them less likely to unfold). Consider the cases shown schematically below for two variants of the same protein. In case #1 the disulfide forms between Cys residues that have been introduced near the protein N- and C-termini, and in case #2 the disulfide forms between Cys residues that have been introduced in the middle of the protein sequence. Which protein is likely to be more stable? (Note: Assume the disulfide bond is intact in both the unfolded and folded states). Explain your reasoning.

SEE MORE QUESTIONS

Recommended textbooks for you

Human Heredity: Principles and Issues (MindTap Co…

Biology

ISBN:

9781305251052

Author:

Michael Cummings

Publisher:

Cengage Learning