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Which separation technique is the most specific and offers the highest protein purification possible?
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- In which of these columns does the RED protein show the greatest retention?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…what is The method that would be BEST to use to monitor protein secondary structure during the titration of a denaturing agent?
- Which layer (aqueous or organic) will phenylalanine partition into during extraction? water or diethyl ether4) Draw a titration curve for the tetrapeptide Trp-Asp-Lys-Gly. Label all pK,s, the pl and the net molecular charges at pH 1 and pH 14 on the graph with their values.If an association between an exposure and an association is differs significantly in strata of a third variable there is an interaction between an exposure and that third variable. O True O False
- 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.I did not understand soultion for the question.. The relationship between Affinity and Association & Dissociation Constant. Four proteins (A-D) all bind the same ligand (X), with different affinities. For protein A & B we know that they have a binding site for X with a Kd (dissociation constant) of 10⁻⁵and 10⁻⁸ M, respectively. For protein C and D we know that they have a binding site for ligand X with a Ka (association constant) of 10³and 10⁵M, respectively. Which protein has the highest affinity for ligand ? Explain your reasoning. How do you make them all in same constant so that values can be compared and the one with highest Ka or lowest Kd (Highest affinity in both cases) can be ruled out.5 ased on molecular weights of purified (no beta-Me) and (beta-Me) sample, which are 97.4 kDa and 47.2 kDa, what can be said about the number and size of the protein monomers, as well as the nature of the bonds holding together the complete quaternary structure of the proteins?
- Please enumerate and explain 1. WHAT ARE THE GENERAL RULES IN GRAMS STAINING CLASSIFICATION OF BACTERIA?5. Draw a schematic illustrating the overall iteration process for solid phase peptide synthesis. You do not need to use specific chemical structures, but your overall depiction should be clear.N-(2-hydroxyethyl)piperazine-N'-(2-ethanesulfonic A purified protein is in a Hepes acid) buffer at pH 7 with 375 mM NaCl. A dialysis membrane tube holds a 2.0 mL sample of the protein solution. The sample tube floats in a beaker containing 1.00 L of the same Hepes buffer, but with 0 mM NaCl, for dialysis. Small molecules and ions (such as Na+, Cl, and Hepes) can to diffuse across the dialysis membrane, but the protein cannot. Assume there are no sample volume changes during the dialysis. Calculate the final concentration of NaCl in the protein sample once the dialysis has come to equilibrium. Calculate the final NaCl concentration in the 2.0 mL protein sample after dialysis in 150 mL of the same Hepes buffer, with 0 mM NaCl, twice in succession. [NaC1] after a single dialysis: [NaCl] after a double dialysis: x10' TOOLS mM mM