PRESCOTT'S MICROBIOLOGY
11th Edition
ISBN: 2818440045677
Author: WILLEY
Publisher: MCG
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Chapter 18.5, Problem 3MI
Summary Introduction
In tandem mass spectrometry, the collection of protein fragments is run through the two mass spectrometers in a sequential manner. This forms the difference between the mass spectrometry and tandem mass spectrometry. In this method, the first spectrometer separates the proteins and fragments which are to be fragmented further. Then, the second spectrometer determines the amino acid sequence of each of the smaller fragments on the basis of the molecular weight. Thus, this technique uses two mass analyzers that are combined in series in order to select the protein.
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Suppose that the sequence is part of a larger globular protein.
Consider the probable location, either on the external surface
or the interior of the protein, of each of the amino
acid residues.
The table gives the hydropathy index values for selected
amino acids in the peptide.
Amino acid
Hydropathy index
alanine
1.8
isoleucine
4.5
threonine
-0.7
glutamine
-3.5
lysine
-3.9
aspartate
-3.5
What is the fraction of the peptide that has the N-terminal amino group deprotonated at pH 9. Please show your answer as a percent of deprotonated N-terminal species relative to all (protonated and deprotonated) N-terminal species.
Can you show your calculations so I can understand your method of approach?
Assume you were given a mixture consisting of one molecule each of all possible sequences of a smallish protein of molecular weight 4800 daltons. If the average molecular weight of an amino acid is, say, 120 daltons, how much would the sample weigh? How big a container would you need to hold it?
Chapter 18 Solutions
PRESCOTT'S MICROBIOLOGY
Ch. 18.1 - MICRO INQUIRY What is the function of the 3-OH...Ch. 18.1 - MICRO INQUIRY Why is it important that identical...Ch. 18.2 - MICRO INQUIRY Which step (or steps) in this...Ch. 18.2 - Retrieve, Infer, Apply Why is the Sanger technique...Ch. 18.2 - Retrieve, Infer, Apply Explain the difference...Ch. 18.2 - Retrieve, Infer, Apply Why does reversible chain...Ch. 18.2 - Prob. 4CCCh. 18.2 - Retrieve, Infer, Apply Suggest a medical and an...Ch. 18.3 - Retrieve, Infer, Apply NGS techniques are...Ch. 18.3 - Retrieve, Infer, Apply Examine figure 18.8. How...
Ch. 18.4 - Prob. 1MICh. 18.4 - Prob. 1CCCh. 18.4 - Prob. 2CCCh. 18.4 - Prob. 3CCCh. 18.5 - Figure 18.12 Metabolic Pathways and Transport...Ch. 18.5 - Prob. 2MICh. 18.5 - Prob. 3MICh. 18.5 - Prob. 1CCCh. 18.5 - Retrieve, Infer, Apply How might the following...Ch. 18.5 - Retrieve, Infer, Apply Compare and contrast...Ch. 18.5 - Retrieve, Infer, Apply Why does two-dimensional...Ch. 18.5 - Retrieve, Infer, Apply What is the difference...Ch. 18.5 - Retrieve, Infer, Apply Describe a ChIP-Seq...Ch. 18.7 - Prob. 1MICh. 18.7 - Retrieve, Infer, Apply Cite an infectious disease...Ch. 18.7 - Prob. 2CCCh. 18.7 - Prob. 3CCCh. 18 - Prob. 1RCCh. 18 - Prob. 2RCCh. 18 - Prob. 3RCCh. 18 - Prob. 4RCCh. 18 - Prob. 5RCCh. 18 - Prob. 1ALCh. 18 - Prob. 2ALCh. 18 - You are developing a new vaccine for a pathogen....Ch. 18 - Prob. 4AL
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- The sequence of a 29 aa long peptide can be determined from the following data: Treatment of the peptide with dansyl chloride reveals that the amino-terminal is Val. Trypsin digestion, separation of peptides, and Edmann technique give the sequences for peptide fragments as follows: T-1 V-G-A-H-A-G-E-Y-G-A-E-A-T-E T-2 A-A-W-G-KT-3 V-L-S-P-A-K T-4 T-N-V-Karrow_forwardWhat is the approximate molecular weight of a protein with 682 amino acid residues in a single polypeptide chain?arrow_forwardConsider the following peptide to answer the questions below: A M A K K E S H I F T A I D E What is the total charge of this peptide at pH = 5? What is the N terminal amino acid (full name)? C terminal amino acid? How many fragments would result if this peptide underwent proteolytic cleavage with V-8 protease and what are these fragments (list them)? Would this peptide be a candidate to form an alpha helix? Why or why notarrow_forward
- identify the interaction that may be produced between the side chain of amino acid residues found at the N-terminus and the C-terminus of the peptide. List all possible peptides that can be formed from the given peptide (use three character/letter abbreviations for each amino acid, i.e., Ala-Gly-Val). NOTE: Any excess will be deducted to the correct answers. Be careful in evaluating your answers.arrow_forwardConsider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ? (Select all that apply.) The two peptides have different compositions. The two peptides have different isoelectric points. The two peptides have different titration curves. The two peptides differ in amino acid sequence. [References] If you were to have a mythical amino acid based on glutamic acid, but one in which the hydrogen that is attached to the y-carbon were replaced by another amino group, what would be the predominant form of this amino acid at pH 12 if the pK, value were 10 for the unique amino group? (Select all that apply.) Both of the carboxyl groups are deprotonated. The amino acid-carries a negative 2 charge. The amino acid carries a negative 4 charge. The amino groups are in the form -NH". Both of the amino groups are deprotonated.arrow_forwardUsing proper convention, provide the amino acid sequence for the following peptide.arrow_forward
- с" CH2 CH2 "НaN H с. CH С" CH Нзс CHз ZI о-оarrow_forwardWhy is it important to identify the N-terminal residue(s) of a protein?arrow_forwardUsing the data in Table calculate the average amino acid residue weight in a protein of typical composition. This is a useful number to know for approximate calculationsarrow_forward
- You are in the process of determining theamino acid sequence of a protein and must reconcile contradictory results. In one trial, you determine a sequence with glycine asthe N-terminal amino acid and asparagine as the C-terminal aminoacid. In another trial, your results indicate phenylalanine as theN-terminal amino acid and alanine as the C-terminal amino acid.How do you reconcile this apparent contradiction?arrow_forwardSuppose that there is a protein consisting of two polypeptide chains with the given sequences in the picture. Before performing Edman sequencing method, it is required to identify the protein's amino acid composition first. Explain why it is required to do the said step first before doing Edman sequencing method.arrow_forwardA peptide has the following amino acid composition: 2 Met, 2 Phe, 2 Glu, 1 Arg, 1 Lys, 1 Val, 1 Leu, 1 Gly, 1 Ser Reaction of the intact peptide with dansyl chloride followed by acid hydrolysis creates a derivative of Met. A specific cleavage of the intact peptide produces fragments with the following sequences: Fragment A: Glu-Gly-Lys-Phe Fragment B: Met-Ser-Leu-Arg Fragment C: Met-Val-Glu-Phe Which reagent was used for the specific cleavage? Cyanogen bromide Carboxypeptidase A Trypsin Chymotrypsinarrow_forward
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