Interpret Protein Characterization Data from the Literature

            The mass spectrometer is an important characterization of proteins. Mass spectrometry is generally an analytical approach which is crucial in establishing relative molecular fragments and ions masses (Sullivan, Han, Liu, Mace, Ervin, Koger, Paul Bales, 2009).  This works by the ionizing the gas molecules in order to establish their mass charge. This technique is effective as it utilizes an electric field which helps in the identification of molecule composition since lighter ions are characterized by speed which helps in achieving accuracy.  This technique also helps in the identification of amino acids components (Sullivan, Han, Liu, Mace, Ervin, Koger, Paul Bales, 2009).

            This technique works by analyzing proteins by utilizing spectrometry where protein are broken down into the peptides components.  Trypsin is often used in the digestion of proteins because it cleaves the peptides components and it is highly actives which enable it to tolerate several additives (Sullivan, Han, Liu, Mace, Ervin, Koger, Paul Bales, 2009). The digested proteins are then separated by utilizing phase reverse column by using acetic acid. The ionized proteins are then passed via eluate column which holds peptides as well as solvents.  When the solvents completely evaporates their surfaces which are the charged moves the peptized which are ionized into the mass spectrometer?  Chromatography is used in the mass spectrometer in the introduction of molecules (Sullivan, Han, Liu, Mace, Ervin, Koger, Paul Bales, 2009).

            The peptides are identified by mass fingerprinting of peptides after they are introduced into the mass spectrometer.  This is preferable because of their mass ranges and high rate accuracies. Mass peptides analysis is preferred in the characterization of protein because it is designed is cheaper and is used in characterization (Sullivan, Han, Liu, Mace, Ervin, Koger, Paul Bales, 2009). In addition, this technique is easy when the general proteins have been fully consumed into smaller fragments of proteins. The most used instrument in analyzing mass peptides MALDA time flight because it permits the obtaining of mass fingerprints of peptides at a high speed (Sullivan, Han, Liu, Mace, Ervin, Koger, Paul Bales, 2009).

            Interest proteins are part of the complex mixture of multiple molecules and proteins as they exist in biological medium.  This procedure, therefore, presents major problems as the ionization of large molecules is effective when the complex mixture only entails equal constituent’s amounts. The secondary spectrum mass complex mixture is challenging to interpret because of the high numbers of components mixtures (Sullivan, Han, Liu, Mace, Ervin, Koger, Paul Bales, 2009).  This is therefore influenced by the fact that digestion of enzyme proteins leads to the rise of numerous peptides number. Multiple phases of analysis of the peptides masses can thus be accomplished with personal mass spectrometer components which are separated by a single space or by a mass spectrometer with separation of time. In the identification of the protein structure characteristics which are indicative of the three structures of dimensions of proteins with the incorporation of mass spectrometry in numerous ways (Sullivan, Han, Liu, Mace, Ervin, Koger,  Paul Bales, 2009).

            Reagents are used in Characterization of the protein compound and the congress by utilization of MS has several importances over the biophysical techniques because of the resolution and the inherent sensitivity of MS (Sullivan, Han, Liu, Mace, Ervin, Koger, Paul Bales, 2009).  The application of MS incorporation with electrospray ionization in the measurements of large protein complexes is furthered by the improvement of sensitive analyzers like the time flight analyzer. In addition, the technique is also effective because the protein being utilized is digested fully if added in small portions and the peptides that exist in either big or small sizes can be analyzed (Sullivan, Han, Liu, Mace, Ervin, Koger,  Paul Bales, 2009).  If the sequence frequency of the analysis is therefore 70% coverage this, therefore, means that the process was thus successful in measuring the protein interests from the figures utilized.

 

 

 

            Reference

Sullivan P.M, Han B., Liu F., Mace B.E, Ervin J.F, Koger D., Paul S., Bales K.R.(2009). .Reduced Levels of Human Apoe4 Protein in an Animal Model of Cognitive Impairment.          Pdf