Homework Answers
molecular weight of albumin 66.5 kDa
molecular weight of myoglobin 16.7 kDa
molecular weight of haemoglobin 1600 kDa
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1d. Finally, you run SDS-PAGE in the presence of 2-mercaptoet urun SDS-PAGE in the presence of...
You have a solution containing human myoglobin (16.7 KD, pi7.0), hemoglobin (64.5 KD; pi7.1). and serum...
You have a solution containing human myoglobin (16.7 KD, pi7.0), hemoglobin (64.5 KD; pi7.1). and serum albumin (66,5 KD: pl 4,9). You want to separate these proteins and you run one portion of the solution through anion exchange chromatography at pH 8 and a second portion of the solution through gel filtration. You measure the protein concentration in fractions collected from both columns and you get the following elution profiles Anion Exchange filtration Protein Concentration Eurim Volume Elution Volume Based...
Confused on how to answer questions E, F, and G. The answer for E is Cysteine,...
Confused on how to answer
questions E, F, and G.
The answer for E is Cysteine,
F (i) is 2
F (ii) is 2
F (iii) is 180
Question 5. Protein X, a protein that binds tyrosine tightly, can be purified in three chromatography steps: 1) affinity chromatography using a tyrosine resin, 2) gel filtration chromatography using a resin with a separation range of 30-200 kDa, and 3) anion exchange chromatography run at pH 7.6. The elution profiles for Steps...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation of the protein is necessary so that proteins run proportionally to their size, based on the interaction of SDS with the unfolded protein. Heat is used to hydrolyze the peptide bonds of the protein. The heat step allows the proteins to unfold, enabling the protein chain to be coated with SDS molecules. Heat is used to hydrolyze disulfide bonds. QUESTION 2 1.5 points Saved...
this is whst i have so its mire spread out. im not sure what else to...
this is whst i have so its mire spread out. im not sure what
else to add.. whst should i be looking for?
koa AB Top of Resolvine 200 116 31 22 14 WellA: MW (Protein Ladder). Well B: Sample Protein 1. Well : Sample Protein 2. Dye front Activities: Based on the picture of the destained SDS-PAGE gel, complete the following Information: -Migration distance of dye front: mm. Molecular Weight Log (MW) Distance travelled Ri (Da) of protein (mm)...
The Jounal of Immunol nes of the National Academy of Sciences USA 89. 6550-6554. 01992, by permis...
explain figure 2 please on the third page
The Jounal of Immunol nes of the National Academy of Sciences USA 89. 6550-6554. 01992, by permision of Proc. Natl. Acad. Sci. USA Vol. 89, pp. 6550-63554, July 1992 Immunolog A 39-kDa protein on activated helper T cells binds CD40 and transduces the signal for cognate activation of B cells RANDOLPH J. NOELLE时, MEENAKSHI ROY.. DAVID M. SHEPHERD., IVAN STAMENKOVICt JEFFREY A. LEDBETTER, AND ALEJANDRO ARUFFo Departmend Microbiology. Dartmouth Medical School One...
You have a solution containing human myoglobin (16.7 KD, pi7.0), hemoglobin (64.5 KD; pi7.1). and serum albumin (66,5 KD: pl 4,9). You want to separate these proteins and you run one portion of the solution through anion exchange chromatography at pH 8 and a second portion of the solution through gel filtration. You measure the protein concentration in fractions collected from both columns and you get the following elution profiles Anion Exchange filtration Protein Concentration Eurim Volume Elution Volume Based...
Confused on how to answer
questions E, F, and G.
The answer for E is Cysteine,
F (i) is 2
F (ii) is 2
F (iii) is 180
Question 5. Protein X, a protein that binds tyrosine tightly, can be purified in three chromatography steps: 1) affinity chromatography using a tyrosine resin, 2) gel filtration chromatography using a resin with a separation range of 30-200 kDa, and 3) anion exchange chromatography run at pH 7.6. The elution profiles for Steps...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation of the protein is necessary so that proteins run proportionally to their size, based on the interaction of SDS with the unfolded protein. Heat is used to hydrolyze the peptide bonds of the protein. The heat step allows the proteins to unfold, enabling the protein chain to be coated with SDS molecules. Heat is used to hydrolyze disulfide bonds. QUESTION 2 1.5 points Saved...
this is whst i have so its mire spread out. im not sure what
else to add.. whst should i be looking for?
koa AB Top of Resolvine 200 116 31 22 14 WellA: MW (Protein Ladder). Well B: Sample Protein 1. Well : Sample Protein 2. Dye front Activities: Based on the picture of the destained SDS-PAGE gel, complete the following Information: -Migration distance of dye front: mm. Molecular Weight Log (MW) Distance travelled Ri (Da) of protein (mm)...
explain figure 2 please on the third page
The Jounal of Immunol nes of the National Academy of Sciences USA 89. 6550-6554. 01992, by permision of Proc. Natl. Acad. Sci. USA Vol. 89, pp. 6550-63554, July 1992 Immunolog A 39-kDa protein on activated helper T cells binds CD40 and transduces the signal for cognate activation of B cells RANDOLPH J. NOELLE时, MEENAKSHI ROY.. DAVID M. SHEPHERD., IVAN STAMENKOVICt JEFFREY A. LEDBETTER, AND ALEJANDRO ARUFFo Departmend Microbiology. Dartmouth Medical School One...
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