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- About a decade ago, it was more common to use peptide mass mapping to identify a protein cut from a gel. Peptide mass mapping involves digesting the protein with trypsin and then measuring the peptide masses using MALDI-TOF mass spectrometry. The more superior method of identifying a protein from a gel is to digest the protein with trypsin and then use liquid chromatography to separate the peptides. The separated peptides are then electrosprayed into a tandem mass spectrometer. The MS-MS data is uploaded into a database such as MASCOT for protein identification. Explain why the LC-MS-MS method is superior to the peptide mass mapping method.A protein consists of two types of peptide chains (A and B) with an unknown stoichiometry (AxBy). When you ran this protein directly on reversed phase-HPLC with UV monitor set at 280 nm, two peaks were resolved. Mass spec determined that the peaks represented Chain A and Chain B, respectively. The peak area is 500,000 for Peak A (Chain A) and 100,000 for Peak B (Chain B). The molecular masses of Chain A and Chain B are 25,000 and 5000, respectively. The extinction coefficients for Chain A and Chain B are 1 mL/mg.cm and 0.5 mL/mg.cm, respectively. Please calculate x/y.macollege.instructure.com/courses/352/pages/covid-proteins-lab-manual?module_item_id=D44333 A = abc Where "A" is absorbance, "a" is molar absorptivity, "b" is the path length (length of the cuvette in units of cm), and "c" is concentration (mol/L). The molar absorptivity is an intrinsic property of a molecule which tells us how intensely it will absorb at a particular wavelength. If "A" is a unitless quantity, "b" is in units of cm, and "c" is in units of mol/L, then what are the units of molar absorptivity? Do a little research to learn how alpha-helices and beta-sheets are drawn in protein structures. If most of the absorption properties are coming from the alpha-helices in these proteins, and many alpha-helices have similar absorbance properties across different proteins, which protein would you predict would have the highest molar absorptivity? Your job is to use the following data table to determine the molar absorptivity for each of the following proteins at their respective…
- 4mL of diluted protein solution was prepared by mixing 200uL of the protein solution with 3.8mL of distilled water. 100uL of this diluted was then mixed with 900uL of Lysozyme solution. Lysozyme activity was measured at 450nm and gave a reading of -0.080 (Abs/min). Calculate the concentration of lysozyme activity in units of abs/min/mL.The following data were obtained for four compounds separated on a 20 m capillary coloumn. Compound t,(min) w(min) A 8.04 0.15 B 8.26 0.17 C 8.43 0.18 (a)Calculate the number of theoretical plates for each compound and the average number of theoretical plates for the column. (b) calculate the average height of theoretical plates. (c) explain why it is possible for each compound to have a different number of theoretical plates?A dimeric binding protein has a KD1 of 50 nM and a Hill coefficient of 1.4. What is the fraction of the protein that has ligand bound at 17 nM concentration of ligand?
- At what distances do hydrogen bonding, hydrophobic interactions and charge transfer interactions act to dominate the interactions between particles when at the isoelectric point? The options are Short range or Long range.How would you make 2.0 L of electrotransfer buffer for transferring the proteins from a gel onto nitrocellulose? Its composition is the following in water: 25 mM Tris (this is a solid; MW = 121) 192 mM Glycine (this is a solid; MW = 75.07) 20.0 % Methanol (you have 100% from the stockroom)Briefly explain the principle behind the following techniques:(a) ion-exchange chromatography (b) gel filtration chromatography (c) affinity chromatography (d) Use three diagrams to illustrate the separation of three different proteins by thesemethods.
- If a particular 150 amino acid polypeptide is known to sample 4 preferred states as it folds into its native protein conformation, and if 10¹5 conformations can be sampled per second, then how many hours would it take for this protein to fold according to Leventhal? 8 × 10107 07 x 10⁹⁰ 4 x 1023 6 x 10¹7Most of the ultraviolet absorption of proteins at 280 nm is due to their content of a. Glutamate b. Tryptophan c. Alanine d. AspartateThere are two proteins in a pH 7 buffer, what you know is: one has a lot of Asp and Glu, the other one has a lot of Lys, Arg and His. Below which approach will get the two proteins separated? salting out affinity chromatography ion exchange chromatography O gel filtration chromatography ultracentrifugation