4 Using Edman's degradation and mass spectrometry, a polypeptide is cut into the followingfragments:ChymotrypsinTrypsinASHREKGQATARGYMATSLARARMTKNVWNVWASHRMКАСEGQATARMATSLGYMKMTKACEEKa) What was the full peptide sequence before degradation?b) Paula thought she forgot to treat her peptide sample with iodoacetate but was relieved tosee the results. What could have gone through her mind?

Edmans degradation is a method of sequencing the amino acids in the peptide. In this first step…

Answered: a) What was the full peptide sequence…

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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You are analyzing the peptide ala-ile-glu-lys-phe-val- tyr-cys. If you treat the peptide with chymotrypsin, which technique would be best to separate the fragments? O a. ultracentrifugation O b. affinity chromatography O c. dialysis d. gel filtration chromatography O e. ion exchange chromatography What is an advantage of NMR spectroscopy over x-ray crystallography in studying protein structure?
Finally, the researcher incubates the peptide with chymotrypsin for two hours at 10 °C and analyzes the products using chromatography. Complete chymotryptic digestion of the peptide with chymotrypsin followed by chromatography yields free tyrosine and free leucine, plus a tripeptide containing Phe and Gly in a 1:2 ratio. Give the final sequence for the peptide based on the results of the acid hydrolysis, dansyl chloride reaction, and chymotryptic digestion. Use the three-letter amino acid abbreviations separated by hyphens for your answer. peptide sequence:
Which technique is used to identify an unknown protein ?
Suppose you have a cell-lysis sample containing genomic DNA, a complex mixture of proteins, and debris. Describe different commonly used analytical methods to i) analyze the molecular masses of the protein mixture. ii) detect the composition (what specific amino acids are there in what proportion) of a specific protein from the mixture. iii) deduce the sequence of some particular proteins from the mixture content
What are some advantages of sequencing peptides by mass spectrometry rather than by Edman degradation?
What is the isoelectric point of this fragment? DHVTHLRKMG
If the target protein is 0.1% of the total protein in the original mixture, a three-step purification process requires: Group of answer choices a 100-fold purification at each step a 22-fold purification at each step a 10-fold purification at each step a 5-fold purification at each step
A peptide was analyzed with the following results. Whatis the primary sequence of the peptide? Briefly state the conclusions of each experimental result and indicate your logic. a)Mass spectrometry was consistent with a peptide of 7 amino acids containing W,C,D,M,N,K, and I. b)One cycle of Edman degradation of the peptide yielded a single product, the PTH derivative of I c)Cleavage of the peptide with CNBr yielded two products. One contained 5 amino acids, and the other 2. One cycle of Edman degradation yielded the PTH derivatives of Iand N, respectively. d)Treatment of the peptide with trypsin yielded 2 products. One of them had significant light absorbance at 280 nm, and Edman degradation yielded the PTH derivative of I. The other trypsin-generated product contained 4 amino acids, and Edman degradation yielded the PTH derivative of Asp.
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
) In urea assay (Catalog #K375-100) what is the nmol (range) it can detect?
You wish to purify a 55 kDa protein, but it is currently present as a mixture with another protein of approximately the same size. Briefly explain a purification strategy that you could use that would enable you to separate the two proteins.
A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin, and the other with cyanogen bromide. Given the following sequences of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment: Asn-Thr-Trp-Met-Ile-Lys Gly-Tyr-Met-Gln-Phe Val-Leu-Gly-Met-Ser-Arg Cyanogen Bromide treatment: Gln-Phe Ile-Lys-Gly-Tyr-Met Ser-Arg-Asn-Thr-Trp-Met

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a) What was the full peptide sequence before degradation? b) Paula thought she forgot to treat her peptide sample with iodoacetate but was relieved to see the results. What could have gone through her mind?