Why doesn't mass spectrometry identify all of the peptides produced when a protein is digested by...
Why doesn't mass spectrometry identify all of the peptides produced when a protein is digested by trypsin?
Homework Answers
Question
Mass spectrometry is the method of separation of proteins according to the mass to charge ratio by converting them to ions. The trypsin is a protease enzyme use in mass spectrometry to break the proteins into small peptides or single amino acid due to its high proteolytic activity. But trysin is not able to identify all the proteins when the protein get digested because:
I. Digestion of proteins by trypsin enzyme is rarely complete.
II. The proteolysis of tightly folded proteins is not accomplished by trypsin enzyme.
III. Many reagents used with trysin enzyme in mass-spectrometry inhibit proteolysis by trypsin enzyme.
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Why doesn't mass spectrometry identify all of the peptides
produced when a protein is digested by...
5. An unknown human protein was digested with the enzyme trypsin and the mixture of the...
5. An unknown human protein was digested with the enzyme trypsin and the mixture of the resulting tryptic peptides were analysed by MALDI-TOF/TOF mass spectrometry. A TOF MS spectrum of the peptide mixture and three MS/MS fragmentation spectra from the three most intense peptide ions have been collected. Explain how this protein could be identified.
5. An unknown human protein was digested with the enzyme trypsin and the mixture of the resulting...
5. An unknown human protein was digested with the enzyme trypsin and the mixture of the resulting tryptic peptides were analysed by MALDI-TOF/TOF mass spectrometry. A TOF MS spectrum of the peptide mixture and three MS/MS fragmentation spectra from the three most intense peptide ions have been collected. Explain how this protein could be identified.
1st attempt When using tandem mass spectrometry for peptide sequence determination, what is the input into...
1st attempt When using tandem mass spectrometry for peptide sequence determination, what is the input into the second mass spectrometer from the collision chamber? Choose one: A. Peptides from a select range of masses B. Tryptic fragments of the protein of interest C. Isolated and fragmented peptides D. Whole protein
What peptides are expected to be produced when a-melanotropin (SerTyro Ser Met GluHis Phe Argo TrpoGlyolyProVal)...
What peptides are expected to be produced when a-melanotropin (SerTyro Ser Met GluHis Phe Argo TrpoGlyolyProVal) is cleaved by Part A trypsin Enter your answers separated by a comma(s). Name peptides using the one-letter abbreviations. Submit Request Answer Part B cyanogen bromide Enter your answers separated by a comma(s). Nume peptides using the one letter abbreviations, Subm Request Answer
You have isolated the proteins from two other adjacent spots after 2D electrophoresis and digested them...
You have isolated the proteins from two other adjacent spots after 2D electrophoresis and digested them with trypsin. Following MALDI-TOF mass spectrometry, the 2 two proteins were found to be identical except for one peak. For this peak, the mass-to-charge ratio (m/z) values differed by 80 g/mol (or daltons), a value that does not correspond to any discrete difference in amino acid sequence. (For example, glutamic acid i instead of valine at one position would give an m/2 ーーーーーーーーーーーーーーー difference...
What peptides are expected to be produced when an unknown hormone (Cys−Ala−Phe−Met−Gly−Asp−His−Arg−Ala−Cys−Lys−Pro−Val) is cleaved by: a)...
What peptides are expected to be produced when an unknown hormone (Cys−Ala−Phe−Met−Gly−Asp−His−Arg−Ala−Cys−Lys−Pro−Val) is cleaved by: a) trypsin b) cyanogen bromide c) thermolysin
Biochemistry project 2 To have manageable peptides for sequencing by Edman Degradation, you first reduced all...
Biochemistry project 2 To have manageable peptides for sequencing by Edman Degradation, you first reduced all of the disulfide bonds and then digested the protein with cyanogen bromide. You then isolated one of the peptide fragments from this digest by isoelectric focusing, split it into two aliquots, and subjected one aliquot to tryptic digest and one aliquot to chymotryptic digest. After isolating all of the peptides from these digests, you sequence the peptides. The following are the sequences you obtained...
When plasmid pD21 is digested with the following enzymes, these bands are produced (all in kb):...
When plasmid pD21 is digested with the following enzymes, these bands are produced (all in kb): HinIII : 3.82, 0.18 SaII : 2.35, 1.65 EcoRV : 3.0, 1.0 HindIII + SaII : 2.35, 1.20, 0.27, 0.18 HindIII + EcoRV : 1.87, 1.00, 0.95, 0.18 SaII + EcoRV : 1.60, 1.40, 0.75, 0.25 Draw a restriction map based on the fragments that were produced.
Could we have used Mass Spectrometry after the GC analysis (GC-MS) to identify which peak on...
Could we have used Mass Spectrometry after the GC analysis (GC-MS) to identify which peak on the GC was which isomer? Why or why not?
This is for a biochemistry class. Thanks 7. How is phenyl Isothiocyanate useful in determining protein...
This is for a biochemistry class. Thanks
7. How is phenyl Isothiocyanate useful in determining protein structure? 8. The absorption coefficient of bovine immunoglobulin at 280 nm is 210,000 M cm What is the absorbance of a 0.1 mg ml solution across a 1-cm path? What percentage of the incident light is transmitted by this solution? (Hint: check question 3.4 in the textbook) 9. The relative electrophoretic mobilities of a 30-kDa protein and a 92 kDa protein used as standards...
1st attempt When using tandem mass spectrometry for peptide sequence determination, what is the input into the second mass spectrometer from the collision chamber? Choose one: A. Peptides from a select range of masses B. Tryptic fragments of the protein of interest C. Isolated and fragmented peptides D. Whole protein
What peptides are expected to be produced when a-melanotropin (SerTyro Ser Met GluHis Phe Argo TrpoGlyolyProVal) is cleaved by Part A trypsin Enter your answers separated by a comma(s). Name peptides using the one-letter abbreviations. Submit Request Answer Part B cyanogen bromide Enter your answers separated by a comma(s). Nume peptides using the one letter abbreviations, Subm Request Answer
You have isolated the proteins from two other adjacent spots after 2D electrophoresis and digested them with trypsin. Following MALDI-TOF mass spectrometry, the 2 two proteins were found to be identical except for one peak. For this peak, the mass-to-charge ratio (m/z) values differed by 80 g/mol (or daltons), a value that does not correspond to any discrete difference in amino acid sequence. (For example, glutamic acid i instead of valine at one position would give an m/2 ーーーーーーーーーーーーーーー difference...
This is for a biochemistry class. Thanks
7. How is phenyl Isothiocyanate useful in determining protein structure? 8. The absorption coefficient of bovine immunoglobulin at 280 nm is 210,000 M cm What is the absorbance of a 0.1 mg ml solution across a 1-cm path? What percentage of the incident light is transmitted by this solution? (Hint: check question 3.4 in the textbook) 9. The relative electrophoretic mobilities of a 30-kDa protein and a 92 kDa protein used as standards...
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