Is there more than one subunit shown? Is your protein bound to anything else? Describe the secondary structures you see.
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Is there more than one subunit shown?
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Is your protein bound to anything else?
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Describe the secondary structures you see.
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- Define the following terms:a. protein motifb. conjugated proteinc. dyneind. zwitterione. electrophoresisPlease explain!!! select all that are right the same Protein X was purified from tissue source A and tissue source B, yielding the following results: Protein X, sample A: specific activity = 100 U/mg; fold-purification = 200 Protein X, sample B: specific activity = 1000 U/mg; fold-purification = 100 Which of the following statements are correct? a) Protein X, sample A has a higher level of purity than Protein X, sample B. b) Protein X, sample B has a higher level of purity than Protein X, sample A. c) Tissue source A has a higher specific activity for Protein X than tissue source B. d) Tissue source B has a higher specific activity for Protein X than tissue source A.In SDS-PAGE. What chemical is used to ensure that all protein molecules are coated with a negative charge? IPTG. β-mercaptoethanol. X-Gal. SDS.
- A protein was purified and then analyzed on a size exclusion column. Its MW was determined to be 50,000 Dalton. The SDS-PAGE gel shows two bands, corresponding to molecular weights of 10,000 and 15,000 Dalton. Describe the native conformation of this protein in terms of the number of subunits present and their molecular weight.Need help, please. Answer choices are provided below for drop-down questions. 1. The overall charge of this protein at pH 7 is Drop-down answer choices are [positive, negative, or neutral] 2. In the first dimension of 2-D PAGE, this protein's isoelectric focusing point is Drop-down answer choices are [between 4 and 6, between 6 and 8, or between 8 and 10] 5. A mole of the above protein weighs ____ g. For 1 mL of a 5 mM solution of the above protein, you would need to weigh out ____ Drop-down answer choices are [g, mg, mcg, ng, or pg] (number and unit, at least one non-zero integer to the left of the decimal point, don't round)What is the method of MS protein quantification presented here? Please answer very soon will give rating surely Complete Answer needed
- What is the function of sodium dodecyl sulfate (SDS) in SDS-PAGE? stabilizes the gel matrix, improving resolution during electrophoresis SDS solubilizes proteins to give them uniformly negative charges, so the separation is based purely on size. SDS raises the pH of the gel, separating multiunit proteins into individual subunits. SDS solubilizes proteins to give them uniformly positive charges, so separation is based purely on pH.topic: Bradford AssayThere are numerous methods of protein determination in use, but this module focuses on the Bradford assay.The Bradford assay is a dye-binding method that employs Coomassie Brilliant Blue G-250, whose structureis shown in Figure 2.3.4.1. Coomassie Brilliant Blue G-250 is a dye that interacts with proteins throughhydrophobic and electrostatic interactions. What are the identities and functions of the components of the Bradford reagent in protein contentdetermination?. Pick all that are TRUE regarding analysis of quaternary structures of proteins using polyacrylamide electrophoresis:I. The added β-mercaptoethanol disrupts S--S bonds bridging the polypeptide chains causing the appearance of higher Rf bands compared to the native protein run. II. Heating up any protein before subjecting to SDS-PAGE will always result in the formation of more than one band.III. A good asymmetrical gel layout would be : (Lane 1) MW ladder, (2) native protein, (3) protein + β-ME, (4) protein + HCL, (5) protein + β-ME + HCl.IV. Formation of a single band in the protein + β-ME + HCl run, whose Rf is lower than the native run, could be indicative that the protein is a homodimer.A. I onlyB. I and IIC. II and IIVD. None is true
- The A280 of a protein sample loaded onto a gel was determined to be 0.767 (1.00 cm path length, after subtracting the blank). The total volume of this sample was 428 µL. 19.0 µL of this protein sample was mixed with 19.0 µL of 2X laemalli sample buffer and then 12.0 µL of the entire sample was loaded into the gel and electrophoresed. Calculate the amount of protein that was loaded into the gel (in µg).1. Search for the `P06858` a) Give information about the PTM and Processing of this protein. b) Which position has maximum amount of variations? Give details about the variations. (Eg: What kind of variation? Feature ID? Disease association? etc..)a 2D gel electrophoresis was done on the proteins found in the chart. create a chart with the correct parameters on both dimensions using 1-6 to indicate the position of each protein on teh 2D gel.