Why do you have to run a standard in MALDI-ToF mass spectrometry when evaluating the size...
Why do you have to run a standard in MALDI-ToF mass spectrometry when evaluating the size of proteins?
Homework Answers
MALDI-ToF mass spectrometry is done for evaluating the size of proteins because of the following reasons-
1. In this analytical technique the protein samples are ionized into charged molecules or ions by absorbsion of energy from ultraviolet lasers by the matrix. The ratio of their mass-to-charge (m/z) is measured by this technique.
2. The ion source used here is matrix-assisted laser desorption/ionization or MALDI. Time-of-flight (TOF) is used as the mass analyzer.
3. Another advantage of this technique is it allows minimal fragmentation of the samples.
4. MALDI-TOF MS is less susceptible to impurities like buffer, salts, detergents and contaminants, and permits intact mass determination of the protein with adequate accuracy. The sample preparation requires less time.
5. This technique has high sensitivity and the analysis is also vey quick.
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Why do you have to run a standard in MALDI-ToF mass spectrometry
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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...
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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...
The compounds have the same molecular mass. How can you use mass spectrometry to distinguish them. Draw two of the possible ions that results when the molecular ion of the following either undergoes fragmentation by a cleavage. Use the synthesis of Williamson to prepare the following ether
Mass Spectrometry: can someone explain how the heck I do this
problem? It's French to me.
Use the data below from an electron impact mass spectrum of a pure compound to deduce its structure. Draw your structure in the drawing window. Data selected from the NIST Web Book. You do not have to consider stereochemistry. You do not have to explicitly draw H atoms. In cases where there is more than one answer, just draw one.
25-25. Chromatography-mass spectrometry. Cocaine metabolism in rats can be studied by injecting the drug and periodically withdrawing blood to measure levels of metabolites by HPLC-mass spectrometry. For quantitative analysis, isotopically labeled internal standards are mixed with the blood sample. Blood was analyzed by reversed-phase chro- matography with an acidic eluent and atmospheric pressure chemical ionization mass spectrometry for detection. The mass spectrum of the collisionally activated dissociation products from the m/z 304 positive ion is shown in the figure on...
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