CUSTOM PRESCOTT'S MICROBIOLOGY
11th Edition
ISBN: 9781266032844
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
How long is a fully extended peptide chain that contains the same number of amino acids?(The distance between consecutive amino acids in a fully extended chain is 3.5 Å; the repeat distance ofan a-helix is 5.4 Å.)
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-K
Chapter 18 Solutions
CUSTOM 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 bacterially produced antibiotic gramicidin A forms channels in cell membranes that allow the free diff usion of Na+ and K+ ions, thereby killing the cell. This peptide consists of a sequence of Dand L-amino acids. The sequence of a segment of fi ve amino acids in gramicidin A is R-Gly-L-Ala-D-Leu-L-Ala-D-Val-R′. Complete the Fischer projection below by adding the correct group to each vertical bond.arrow_forwardYou 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_forwardPartial hydrolysis of a protein yielded a number of polypeptides. One of them was purified. Deduce the sequence of amino acids in this polypeptide from the following information: (a) Complete acid hydrolysis yielded ala + arg + 2ser + lys + phe + met + trp + pro (b) Treatment with fluorodinitrobenzene (FDNB, the Sanger reagent) followed by complete acid hydrolysis yielded dinitrophenylalanine (DNP-ala) and a dinitrophenyllysine (e-DNP-lys) as the only DNP derivatives. (c) Neither carboxypeptidase A nor carboxypeptidase B released a C-terminal amino acid. (d) Treatment with cyanogen bromide (CNBr) yielded two peptides: One contained ser + trp + pro. The other contained all the remaining amino acids (including the second ser). (e) Treatment with chymotrypsin yielded three peptides. One contained only ser + pro. Another contained only met + trp. The third contained phe + lys + ser + arg + ala. (f) Treatment with trypsin yielded three peptides. One contained only ala + arg. Another…arrow_forward
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