I. A protein, X, was Isolated from a pathogenlc mlcroorganism. The proteln Is a vlrulencefactor whose path0genlclty lies In a heptapeptide of unknown sequence. After trypsincleavage of the heptapeptide from protein X, the peptlde's compOsition and sequencewas determined. The fOllowing were the results of the sequenclng process:1. When the peptide was treated with dinitrofluorobenzene (DNFB), DNP-aspand a mixture of amino acids were produced.2. When the same Intact peptide was treated with streptococcal protease, apentapeptide of composition asp, asN, cys, gly and ser and 2 amlno acidswere released.3. When the heptapeptlde was also treated with hydrOxylamine HCI, atripeptide and a tetrapeptide were obtained. The C-terminal amino acid ofthe tripeptide was asN.1) What is the sequence of the heptapeptide if it is composed of cys, asp, lys, asN, glyand ser only?2) What is the pl of the heptapeptide?

Proteins are formed of peptide bonds formed between the amine group and the carboxyl group of the…

Answered: A protein, X, was Isolated from a…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter30: Protein Synthesis

Section: Chapter Questions

Problem 13P

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Similar questions

You are trying to determine the PTMs on your protein of interest, so you set up a mass spectrometry experiment. You get the following data. Starting sequence: PRTEINSKICKASSDER After Trypsin digest, you get the following major peptides and weights from MS: TEINSKICK/1167 Da ASSDER/664 Da a. Which of these peptides is modified? b. What is the modification?
DO NOT COPY OLDER ANSWERS! AND SHOW FULL WORK! I have a mixture of 4 proteins, whose sequences are shown below (note that each protein is a 100-repeat of the sequence shown). Protein A: (Gly-Ala-Lys-Val-Ile-Phe-Glu-Val-Asn-Gly) Protein B: (Ala-Ala-Lys-Arg-Ile-His-Glu-Ala-Asn-Lys) Protein C: (Glu-Val-His-Asp-Ala-Asp-Glu-Val-Asn-Asp) Protein D: (Ala-Lys-Arg-Phe-Trp-Phe-Gly-Ile-Ala-Gly) 1) Which protein/s are MOST LIKELY to precipitate out at a pH of 3.5? a) A b) B c) C d) D e) B & C f) A & D g) None of them h) Cannot be determined.
One of the members of your research group attempted to isolate theenzyme using the protocol you presented. To confirm whether theygot the protein, SDS-PAGE was performed and the gel on the rightwas obtained. Perform the necessary calculations to determine themolecular weight of the suspected band on the gel in the lanelabeled “dialyzed.”
1. Search for the `P06858` a) Give information about the PTM and Processing of this protein. b) Which position has maximum amount of variations? Give details about the variations. (Eg: What kind of variation? Feature ID? Disease association? etc..)
Pathogenic E. coil have recently been shown to degrade tight junction proteins during infection. How would this provide an advantage to the bacteria?
C.Why does 500 mM imidazole result in the elution of a protein with a 6X-His tag?
A protein was purified and then analyzed on a size exclusion column. It's molecular weight was determined to be 40,000 Dalton. The SDS-PAGE gel shows one band, corresponding to a molecular weight og 10,000 Dalton. Describe the native conformation of this protein in terms of the number of subunits present and the molecular weight of the subunits.
PLEASE MAKE THE DR BRUJIN GRAPH From these k-mers construct a de Bruijn graph and determine the sequence of the contig. AGCG ATCT ATGA ATGG ATTC CCCT CCTG CTCT CTGA CTGC CTTT GAAG GATT GCGT GCTC GTTC TATG TCAT TCTA TCTT TGAA TGAT TGGA TGTT TTCA TTCC TTTC
6. Please describe the events that may result in a mature protein not having methionine asthe N-terminal amino acid.
3 i. Define Biological Value (BV) of Proteinsii. What are the advantages of this protein evaluation method when compared to Nbalance and chemical score?5iii. A bull consumes 7 kg DM of feed containing 60 g N/kg. The bull excretes 120 g N inthe faeces and 50 g N in the urine. The feacal and urinary N had 20 g metabolic feacalnitrogen (MFN) and 6 g endogenous urinary nitrogen (EUN) respectively.Calculate the BV of the protein in the diet.
Are there ways to reveal the detailedworkings of a protein machine that donot require the purification of each ofits component parts in large amounts,so that the machine’s functions canbe reconstituted and dissected usingchemical techniques in a test tube?
A researcher has synthesized two peptides and needs to confirm whether the peptides were synthesized with the correct sequence using mass spectrometry. What is the sequence of the b4 and y7 ions for peptide GAMECHANGER? The peptide SLISRAEFLAGVRVGV is digested with trypsin. Then the products of the digestion are subjected to ESI TOF-MS in positive ion mode with the peptides in a pH 2 solution. What peptide fragments will result and what are their m/z?

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