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 vast majority of structures deposited in the Protein Databank (>95%) have been determined using NMR Hard keratins (such as in the skin) are less resistant to stretch because the larger number of disulfide bonds resist deformative forces. Structures produced by X-ray diffraction are as good as the solutions from which they are derived they are false and I know that but explain why they are false
1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
You were able to extract an amino acid sequence from an unknown protein you process through mass spectrophotometry. How will you able to identify the said protein and its function?
Approximate molecular weight for an unknown protein from gel-filtration experiment is 130 kDa. Thirty six mg of this pure protein was treated with excess of fluorodinitrobenzene. After the reaction and complete acid hydrolysis the mixture was found to contain 356 µg of dinitrobenzene derivative of methionine (free acid) and no other amino acid-dinitrobenzene derivatives. Is this protein consisting of single polypeptide chain or multiple subunits? If it consists of multiple subunits, then how many? From these data, can you calculate the molecular weight of the protein more precisely?
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A mixture of five proteins are analyzed by MALDI-TOF. Their molecular weigths are 3 kD, 22 kD, 100 kD, 225 kD and 515 kD. A peak appears in the mass spectrum at 33.3 kD. Which protein most likely gave this peak?
Please explain the results and conclusion based on the results of these two chromatograms (one for proteins and one for nucleic acids). For the proteins chromatogram, the Xs on the line from left to right are: unhydrolyzed protein hydrolyzed protein alanine solution histidine solution aspartic acid solution lysine solution methionine solution a solution containing an unknown amino acid (it will be 1 of the 5 amino acids found in microfuge numbers #3 to #7 above) For the nucleic acid chromatogram, the Xs on the line from left to right are: unhydrolyzed nucleic acid hydrolyzed nucleic acid adenine solution cytosine solution uracil solution adenine-cytosine-uracil solution #1 and #2 for both proteins and nucleic acid chromatogram was prepared with yeast cells and centrifugation. Yeast was grinded down with sand and then TCA (trichloroacetic acid) The yeast contains yeast cells held together with a starchy binding material. Glucan (a cellulose-like polysaccharide) is present in the…
A stock solution contains 0.2 mg/mL protein. From this stock solution, 179 uL is diluted with 1.1 mL buffer. What is the concentration of protein in this dilution?
A number of techniques can separate proteins on the basis of their differences in mass. Describe the use of two of these techniques, centrifugation and gel electrophoresis. The blood proteins transferrin (MW 76 kDa) and lysozyme (MW 15 kDa) can be separated by rate zonal centrifugation or SDS-polyacrylamide gel electrophoresis. Which of the two proteins will sediment faster during centrifugation? Which will migrate faster during electrophoresis?
a) The pl of a protein is 9.0. What will be the net charge (positive, negative or neutral) on the protein under the following conditions: A buffer with pH 9.0: A buffer with pH 7.0: A buffer with pH 10.0: b) Your protein is present in a sample buffer which has a pH 7.0. The sample is applied to an ANION EXCHANGE column. Will protein 1 bind to the beads on the column? Yes/No
Which of the following is NOT a unit of concentration? All of these options are units of concentration. mM Moles/Liter Molar You gathered your data from Lab , and found the following values: Total Activity of lysozyme in HEW: 14 units Total Activity of lysozyme in carb 1: 21 units Total amount of protein in HEW: 70 mg Total amount of protein in Carb 1: 15 mg Calculate the extent of purification of lysozyme in Carb 1. A 7 fold B 150% C 15 fold D 70%
Explain the Rf value obtained on the basis of the structure of amino acids use. Explain in 1-3 sentence only.

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