1. Explain why only small areas of the Ramachandran plot (below) are occupied (shaded grey) and what the two dark grey shaded areas represent in terms of a protein structure. +180 120 60 -60 -120 -180 -180 -120 -60 60 120 +180
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- Which of these nH measurements is indicative of a partially positively cooperative protein? -1 0 1 2A gel filtration column with a fractionation range of 1.5-20 kDa is used to separate out the proteins shown below. If these proteins are collected into separate fractions in between the void volume and total volume, in which order will they elute? Indicate if any of the proteins are found in the void volume or total volume fractions. Protein Z - 3330Da Protein Y - 13kDa Protein X - 1.3kDa I. Total volume fraction II. Third protein fraction III. Second protein fraction IV. First protein fraction V. Void volume fractionTo which of the proteins does peak 4 correspond to? PLEASE EXPLAIN WHY A. A B. B C. C D. D E. B and C
- Two proteins of different molecular weight (mw) are mixed and need to be separated. When eluted through a Sephadex-G50 chromatography column, what is the order of elution (first followed by second)? A. protein with mw of 40 kDa; protein with mw of 20 kDa B. both proteins will elute at the same time C. both proteins will not elute as the combined mw is larger than 50 kDa D. protein with mw of 20 kDa; protein with mw of 40 kDThe limit for G-200 beads is 5000-600,000. When you pass two proteins- Protein A (75, 000), Protein B (1,000,000), through these beads, the protein that will elute out last is – They both elute out at the same time. Protein B Protein AHOW MANY of the following five items represent modes of protein denaturation? 1.) heating a protein sample 2.) cooling a protein sample (slowly) 3.) putting a protein sample in a saltier environment 4.) eating a protein sample (such as with a whisk) 5.) adding acid to a protein sample
- will UPVOTE Kindly answer the question. 1. Do you think free amino acids will give a positive result with the biuret test? Explain why.In order to prepare a standard curve, you will do serial dilutions of the standard protein. Assume the protein concentration in tube A is 3 mg/ml and you take 0.5ml and add it to the next tube (tube B) containing 0.5ml of buffer. What is the concentration in tube B?Why would your protein measurement not match to package label? Let us disregard the idea that the package is wrong. Provide one plausible explanation. Use several sentences to outline your reasoning.
- Give only typing answer with explanation and conclusion You want to make 94 µL of the diluted Cell-Free extract for estimation of total protein. To do this, how much water will you add to the correct volume of the undiluted cell-free extract? Note: Cell-free extracts will need to be diluted 1:25 in water.Find a method that uses some form of HPLC for the analysis of proteins. What was the stationary phase used? How does this kind of stationary phase separate the proteins? What kind of mobile phase was used? Was the method isocratic or was a gradient used? How were the proteins detected?The following protein quantification utilizes Cu ions except fora. Lowryb. Biuretc.Bradford