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

See similar textbooks

Similar questions

What is the minimum length of the column required to completely separate the amino acids? What is the time required for solvent elution (i.e. time for all amino acids to exit the column)?
Jacqueline isolated an interesting new protein from the broth of a yeast culture. After purification of the protein, she requested an amino acid analysis and found that the protein contained 0.57% tryptophan by weight (tryptophan Mr-204). Calculate the minimum molecular weight of the protein (i.e., assuming there is only one tryptophan residue per protein molecule).
A 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 fraction
Marker Proteins Molecular Weight (daltons) Distance 132,000 66,000 43,000 14,400 Serum Albumin (Dimer) Serum Albumin (Monomer) 23mm 32mm Ovalbumin 39mm 60mm Lysozyme Unknown 1 26mm Unknown 2 58mm Rabbit serum (albumin) 33mm 1.On semilog paper (provided below) plot the distance migrated by each standard protein as a function of molecular weight. Determine the molecular weight of the unknown proteins and the major protein found in rabbit serum (albumin) from this calibration curve. ii) Interferon is a protein of 25,000 Dalton. How far would it have migrated, land it been included in this experiment? iii) The average amino acid residue in a protein has a molecular weight of 120 Daltons. Assuming that your unknowns are average, how many amino acid residues do they contain
You have a soluble protein that is highly flexible and is only 23 kDa in size. What is the most suitable technique (X-ray crystallography, NMR, cryo-EM) for structure determination of this protein? Explain your reasoning.
You perform electrophoresis of 3 proteins, Hemoglobin (pl: 6.8), DNA Polymerase (pl: 5.2) and Porcine pepsin (pl: 1.0) in a Tris-Glycine buffer (pH 5.2). (pl = Isoelectric point). Select which of the following is true. O All proteins will migrate at the same rate O All proteins will migrate at the same direction Porcine pepsin will migrate toward the electrode Porcine pepsin will not migrate and stay in the well
In RP HPLC, one of the most common separation methods used to measure purity, strength, dosage, etc, a protein would be put into 0.1% (1000 ppm) TFA (Trifluoroacetic acid), what do you suppose this does to the protein in many cases? (Pick the BEST answer). somewhat denaturing to very denaturing oxidizes cysteine ionizes acid and base groups
How can you separate and identify Molecular weight of target protein from a protein sample?
A typical bacterial DNA has a molar mass of 4 × 109 g m ol-1 . Approximately how many nucleotides does itcontain?
Four proteins Cytochrome C (pI=10.2) Myoglobin (pI=7.2), Hemoglobin (pI = 6.8) and Serum Albumin (pI= 4.8) were used in our gel electrophoresis lab exercise. What is the molecular basis for the differences in the electrophoretic mobilities of the four proteins analyzed in this exercises? size shape charge all of them
You assay 0.5 ml of 1/2000 diluted egg white for protein, as described in the practical schedule, and the spectrophotometer reading at 595 nm is 0.6. Using the attached calibration curve(click to enlarge), calculate the concentration of protein in undiluted egg white. Give your answer in mg/ml.
Predict the amino acid sequence based on the conditions below. Use the one-letter abbreviation of amino acids. a. The amino acid in the C-terminal is optically inactive. b. The fifth amino acid is a neutral aromatic amino acid that yields a negative result for the Xanthoproteic test using intact protein while producing a yellow soln with Xanthoproteic reagent and yielding a negative result with Hopkin's Cole test using basic hydrolysate. c. Yields serine and a hexapeptide after treatment of aminopeptidase (specificity: peptide bond on the N-terminus). d. The amino acid beside the N-terminal a.a. will yield ornithine and urea after alkaline hydrolysis. e. The third amino acid gives a positive result for Hopkins-Cole Test. f. Chymotrypsin cannot cleave the peptide bond on the fifth amino acid because of the presence of this a.a. residue. g. The amino acid at the carboxy-end of the third a.a. will yield a black precipitate for Pb(Ac)2.

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS