The ESI-MS spectrum below was obtained for HEWL. Using peaks 5 and 6, calculate the molecular mass of HEWL. 100- % A13 1101.5 A12 1193.1 A11 1301.4 1310.5 A10 1431.6 A9;1590.6 A8 1789.2 1801.3 1601.4 A7 2044.6 1441.3 2049.7 0- mt 1000 1200 1400 1600 1800 2000 2200 2400
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- A packing plant fills bags with cement. The weight X kg of a bag of cement can be modelled by a Normal distribution with mean 50 kg and standard deviation of 2kg. a) If a bag is selected is at random, find the probability that the weight of the bag is greater than 55 kg. b) If three bags are selected at random, find the probability that 2 bags weigh more than 55 kg. c) Compute the probability in part a using RStudio.If the enzyme maltase has a Vo of 0.25 mM per minute when [S] = 0.10 mM, and a Vo of 0.40 mM perminute when [S] = 0.40 mM, what is its y-intercept on a Lineweaver-Burk plot?A. 0.10 minutes per mMB. 0.20 minutes per mMC. 0.50 minutes per mMD. 1.0 minutes per mME. 2.0 minutes per mMYou and Build Jakapan were tasked to determine the molecular weight of an unknown protein using gel filtration chromatography. You made use of a Sephadex G-100 column with a height of 30.0 cm and an internal volume of 52.0 mL. Initially, blue dextran was made to run through the column, giving an elution volume of 3.0 mL. Next, a calibration mixture containing phytochrome 730 (124 kDa), hemoglobin (64.5 kDa), and horse myoglobin (17 kDa) was made to flow into the column, generating a flow rate of 2.0 mL per minute. Shown as follows is the illustration of the collected fractions. Fraction number: ¯ÐЯ¯¤¤Ðж¶ÐÐ ÐС¡8 1 2 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 Subsequently, a sample of the unknown protein was loaded into the column. The elution profile of the unknown protein is shown below. Absorbance at 254 nm 0.6 0.5 0.4 0.3 0.2 0.1 0 0 2 4 6 8 10 12 14 16 18 20 22 24 26 28 30 32 34 36 38 40 Elution Volume, mL
- Please identify the following on the Michaelis- Menten plot shown A, B, C, and the X and Y axes. Please briefly explain the significance of each. A B сCan you check if A is correct and please help answer the following questions?In a mixed heteropolymer experiment, messages were createdwith either 4/5C:1/5A or 4/5A:1/5C. These messages yielded proteinswith the amino acid compositions shown in the followingtable. Using these data, predict the most specific coding compositionfor each amino acid.4/5C:1/5A 4/5A:1/5CPro 63.0% Pro 3.5%His 13.0% His 3.0%Thr 16.0% Thr 16.6%Glu 3.0% Glu 13.0%Asp 3.0% Asp 13.0%Lys 0.5% Lys 50.0% 98.5% 99.1%
- SDS-PAGE and Agarose gel electrophoresis can both be used to separate proteins or protein- complexes based on their size. Separation of a multi-subunit protein complex by SDS-PAGE resulted in two bands with molecular weights of 86 KDa and 136 KDa, while separation of the same complex using Agarose gel electrophoresis resulted in two bands with molecular weights of 222 KDa and 444 KDa. Based on this information, which of the following statements is most likely to be correct? O The complex has a molecular weight of 222 KDa O The complex exists as a dimer of homo-dimers O The complex exists as a dimer of hetero-dimers SE O The complex exists as a trimer, but the individual protein subunits are covalently crosslinked to each otherPlease answer both asap If there were only 2 tests for COVID-19 and Test A has a high sensitivity but low specificity while Test B has low sensitivity and high specificity, which test would you choose and why? -A Covid-19 diagnostic test has a sensitivity of 80%. What would be the percentage of false negatives for the test?Based on your molecular weight predictions from computational analysis of the DHFR fusion proteins analyzed this semester, what would you estimate the molecular weight of the GST tag used to be?
- A unique aquatic plant was discovered from a lagoon in El Nido, Palawan. To determine the protein content of the plant, an adequate amount of the plant extract was acquired, and Bradford assay was performed. Determine the total protein concentration, in µg/mL, of the acquired plant extract. A bovine serum albumin (BSA) stock solution with a concentration of 250 µg/mL was used and mixtures with the following compositions and absorbance readings were prepared: Volume of BSA (mL) Volume of water (mL) Absorbance Tube # at 595 nm 1 0.00 2.00 0.000 2 0.20 1.80 0.112 3 0.40 1.60 0.225 4 0.60 1.40 0.318 5 0.80 1.20 0.432 6 1.00 1.00 0.551 The absorbance reading of the plant extract is 0.275.The following sequence alignment shows the point mutation that exists in hemoglobin for some cases of sickle cell (HbS) compared to wild type adult hemoglobin (HbA) VLSPADK (HBA) VLSPAVK (HbS) Based solely on the peptide fragment shown, answer the following questions: What is the charge range for the HbA peptide shown above? **Hint, what is convention for how charge ranges are written?? At physiological pH, what is the charge of the HbS peptide? →>>> What is the impact of this point mutation? Choose the letter for the answer choice that best applies. a. Allows for hydrophobic contacts in HbS that lead to higher order structures beyond the a2ß2 heterotetramer b. Allows for ionic interactions in HbS that aids in interactions with solvent c. Destabilizes the ionic interactions of the dimer-dimer interface and prevents the T- to R- state transition d. Prevents the coordination of Fe²+ at the protoporphyrin ringWhen human hemoglobin undergoes a mutation, the mutant protein usually does not replace all of the normal HbA in the red blood cells or erythrocytes of the individual. The erythro- cytes contain mixtures of varying amounts of both HbA and the mutant protein depending on the mutation and the individual. Hb Yakima is a mutant human Hb with an Asp-(B99)His mutation. The diagram on the right shows that Hb Yakima was separated by DEAE-cellulose chromatography from HbA with a 0 – 0.1 M linear gradient of NaCl buffered to pH 8.3. Why is chromatog- raphy carried out at pH 8.3? If the isoelectric point of HbA is 6.85, what is the change in total charge caused by the mutation?How does the change in charge explain the chromatography elution profile of the Hb Yakima/HbA mixture? 1,5 -Hb-A Hb -Yakima 1.0 0.5- 20 40 60 80 00 Fraction number O.D578 nm