please help? its biochemistry What are the masses (in kDa) of some of the most predominate contaminating proteins seen in the purification?
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- Pls help ASAP, thank you! "An alpha-helical structure within a protein is stabilized mostly by"Please ASAP. Thank you. How does the mutation change/affect the structure of the Hb heterotetramer (ie how is quaternary protein structure affected)?Choice and Preparation of a Buffer System1. Choosing the proper buffer solution In Protein Precipitation, two liters of 5mM buffer solution with pH 5.2 is needed in the isolation of albumin. Which among the following buffer solution is best fitted for said purpose? Justify your answer.Buffer solutions pKa Acetate buffer 4.73Tris- (hydroxymethy) aminomethane 8.08Phosphate buffer 7.20 2. Preparation of the chosen buffer system Calculate and measure the amounts (in grams if solid and in mL if liquid) of weak acid and conjugate base needed to be able to prepare the chosen buffer system in part A above. Express your answer in useful units (that is, prepare it from practical amounts or concentrations of starting materials).
- In Multi-Column Purification of rGFP. What happens to the protein amount, protein purity, and/or specific activity of a purification fraction if one of the three is changed? (i.e. understand the relationship between the three.)REFECT AND APPLY Suggest a reason why amino acids are usually more soluble at pH extremes than they are at neutral pH. (Note that this does not mean that they are insoluble at neutral pH.)Qualitative Analysis of Proteins 1. Fill out the table below by providing the necessary information indicated per column. 2. As you have virtually conducted these qualitative tests for proteins, what do you think could be the essential practical or real-life applications of these tests?
- PRECIPITATION OF PROTEINS What are peptides? Do all proteins possess peptide bonds? Do all proteins respond to Biuret’s test? What is the difference between coagulation and denaturation? Why is egg white used as an antidote for lead and mercurial poisoning? Explain its mechanism of action. 4.Why is silver nitrate used in the cauterization of wound? Explain your answer.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−SGBIOCHEMISTRY Why does a dual layer of Cr/Au (20/100nm) delaminate during a GSTAT electrochemical polymerization of PEDOT:PSS?
- pls explain why Which of these CANNOT BE achieved using SDS-PAGE?I. Estimate the MW of a protein.II. Confirm the identity of a protein.III. Confirm the presence of quaternary structure in the protein.IV. Give a qualitative assessment of the protein extract purity.V. Determine the shape of the protein.a. II and Vb. III and IVc. I, III and Vd. I, II, and IV Which of the following statements are TRUE about the discontinuous gel in SDSPAGE?I. The sandwich effect occurs because of the lower mobility of the zwitterionic form of glycine compared to the protein band in the stacking gel.II. Because of the larger pores in the resolving gel, proteins move faster in the stacking gel, but decelerate at the boundary of the two gels.III. In the stacking gel, in terms of net negative charge of the species, the order is: zwitterionic glycine > proteins > chloride ion.IV. The higher pH in the resolving gel allows glycine to carry a more negative charge, resulting in higher mobilities compared to…TOPIC: Precipitation of Proteins by Alkaloidal Reagents 1. In what way can alkaloidal reagents precipitate proteins? ____________________________________________________________________ ____________________________________________________________________ 2. In excess of alkaloidal reagent, did the precipitate formed dissolve or not? What is the evidence for your answer? ____________________________________________________________________ ____________________________________________________________________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…
