Nonspecific elution of affinity bonded macromolecules is used in affinity chromatography explain why?
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Nonspecific elution of affinity bonded macromolecules is used in affinity chromatography explain why?
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- Which nuclear isotope used in protein NMR spectroscopy is the most sensitive to detect? Briefly explain why.Dihedral angles of Phe165 of 4KW4 betasheet values are consistent with what is expected from the Ramachandran Plot?Cone snails are carnivores that inject a powerful set of toxins into their prey, leading to rapid paralysis. Many of these toxins are found to bind to specific ionchannel proteins. Why are such molecules so toxic? How might such toxins be useful for biochemical studies?
- What is the difference of measuring proteins through UV-VIS spectroscopy at 280 nm and at 595 nm with the presence of the Bradford reagent? (note: explain not less than 5 sentences).For paper chromatography, the obtained Rf value of an amino acid with uncharged nonpolar R group is greater than the obtained Rf value of an amino acid with charged polar R goup. TRUE OR FALSE?Using a detailed scheme, propose a step-wise protocol to purify protein B by ion exchange chromatography (Explain your logic/choices).
- In nickel column affinity chromatography，how does the protein binds to column？How is the protein eluted from the column？Fibrinogen contains tyrosine- O - sulfate. Propose an activated form of sulfate that could react in vivo with the aromatic hydroxyl group of a tyrosine residue in a protein to form tyrosine- O -sulfate.Why is ΔG a useful quantity for predicting the favorability of biochemical reactions?
- Why different amino acids have different Rf values? If you separate a mixture of amino acids consist of glutamic acid, histidine, glycine, tryptophan and isoleucine with paper chromatography using NH3: Benzene (10:90) as a mobile phase what do you expect the Rf values of the amino acids will be?VizamylTM is used in brain scans for Alzheimer’s disease. Draw the structure of VizamylTM and identify the radioisotope present in the structure. Explain how F-18 differs from F-19.Hemoglobin is considered to be a tetrameric complex with a 64 kDa (α β)2. When attempting to purify hemoglobin, we must first purify the α and β monomers (about 16 kDa each) to prepare the tetramer. This is formed from the dimer intermediate: 2 α + 2 β -> 2 αβ -> (α β)2. The graph given represents a size-exclusion chromatogram after the refolding of the hemoglobin tetramer Using the size-exclusion chromatogram given, 1. Draw an SDS-Page Gel with a reducing agent such as BME using the three peaks listed on the graph.