A researcher isolates a new protein and finds that it contains 0.755% serine by weight upon amino acid analysis. The molecularmass of serine is 105 g.mol-¹.What is the minimum molecular mass for the protein assuming only one Ser residue per protein molecule?mmin =The researcher estimates the molecular mass of the protein using gel electrophoresis. From this estimated molecular mass, theresearcher concludes the protein contains 3 Ser residues.What is the estimated molecular mass of the protein as shown by gel electrophoresis?g.mol-¹mest =g.mol-1

A peptide is a short chain of amino acid residues linked together via a peptide bond. The peptide…

Answered: A researcher isolates a new protein and…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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).
The following proteins were separated by SDS-PAGE in the presence of mercaptoethanol. Sketch the relative positions of the various polypeptides on the gel. Label the positive and negative ends of the gel.Protein A: 40 kDa single polypeptideProtein B: 80 kDa protein, made up of two subunits of molecular weight 20 kDa and 60 kDa, held together by noncovalent interactionsProtein C: 200 kDa protein, made up of four identical subunits (50 kDa each) linked together by disulfide bonds
This SDS-PAGE loading buffer has SDS (a denaturing detergent), β-mercaptoethanol (a reducing agent), Coomassie Blue (a dye), and glycerol. You will need to dilute your protein samples such that the final concentration of the loading buffer is 1x, meaning that you will add 5 parts of the protein sample for every 1 part of 6x buffer. Calculate how much of the 6x loading buffer you will need to add to each sample. Then, add the appropriate amount of 6x SDS-PAGE loading buffer to the samples. Store the samples in the -20°C freezer. What is the final concentration of glycerol in each of the samples?
A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecularmasses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol, three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein.
A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol, three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein and clearly explain how you came to this determination.
Consider the following protein mixture: Protein A B C D Molecular Weight (kDa) 50 150 200 350 Affinity to Metal ion === Zn²+ === 1. Using hydrophobic interaction chromatography, the protein that will be eluted last is [Select] 2. Using affinity chromatography, the protein that will be eluted last in a Zn²+-containing column is 3. The protein with the fastest migration towards the anode in SDS-PAGE is [Select] IpH value 7 3 9 5 [Select] [Select] 4. Using a buffer solution with a pH of 4, the protein that will bind to an anion exchanger is 5. The protein that will be eluted last in a gel filtration column is [Select] 6. Using isoelectric focusing, the protein that will have a protein band nearest to the cathode (negative electrode) is [Select] % Hydrophobicity 20 45 75 55
Several calibration curves were created for a series of protein standards of known molecular mass using molecular exclusion columns with different pore sizes. Which pore size should be used to perform molecular exclusion chromatography of proteins with a molecular mass near 10,000? 10 µm 5 nm 10 nm 1 pm 100 µm 50 nm 100 nm log (molecular mass) 7- 5mm 5.0 6.0 100 m Lum 10 m 7.0 8.0 9.0 100 um Elution volume (ml) 10.0 11.0 12.0
A protein of unknown structure has been purified. Size-exclusion chromatography reveals that the native protein has a MW of 240,000. Chromatography in the presence of 6 M guanidine hydrochloride yields a single peak corresponding to a protein of MW 60,000. Chromatography in the presence of 6 M guanidine hydrochloride and 10 mM B-mercaptoethanol yields peaks for proteins of MW 34,000 and 26,000. Explain what can be determined about the structure of this protein from these data.
A two-dimensional gel electrophoresis of a protein preparation revealed the presence of five monomeric proteins with the following molecular weights and Isoelectric points: | (10 kDa, pl = 5.6), II (25 kDa, pl = 7.7), III (55 kDa, pl = 5.6), IV (150 kDa, pl = 9.1), V (200 kDa, pl = 8.2). Using native chromatographic conditions which preserve enzymatic activity, what would be the predicted elution order for the five proteins on a gel filtration chromatography column: O1, II, II, IV, V O II, III, I, IV and V OV, IV, III, II, I O IV, V, II, III and I I and III, II, V, IV
A protein has a predicted molecular weight of 47 kDa based on the amino acid sequence, an apparent molecular weight of 50 kDa by SDS-PAGE, and an approximate molecular weight of 95 kDa by size exclusion chromatography. Each of these techniques is described in the appendix. O These results indicate that SDS-PAGE provides the most accurate measure of molecular weight. O These results indicate that the size exclusion chromatography is not very useful at estimating molecular weight. O These results indicate that the protein is a dimer under denaturing conditions. O These results indicate that the protein is a dimer under native conditions. O These results indicate that the protein is cleaved in half under denaturing conditions.
How can I calculate the unknown protein please

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