. What physiological effect would you predict from a mutation that replaced with serine the cysteine in the constant part of the immunoglobulin light chain that is involved in disulfide-bond for- mation with the heavy chain? ,
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- Describe the importance of ubiquitin-dependent degradation of soluble proteins.In TLC, why are the colors of the peaks for each amino acid are different depending on the types of amino acid?Describe the effect of the amino acid change on protein function: how does the HbS protein function differently than the HbA protein in red blood cells?
- provide examples of the levels of protein structure for mevalonate kinase (2HFU) provide the levels of protein structure (primary, secondary, tertiary, etc.) for mevalonate kinase (2HFU)Define the term and describe the autoantibodies presentin SLE.List 4 different actiated carrier molecules, for each one, list both the oxided and reduced forms
- What peptides are expected to be produced when α-melanotropin is cleaved by (a) trypsin, (b) cyanogen bromide, or (c) thermolysin? (as shown)Draw a fractional binding curve for trimeric protien that has a binding site on each subunit. Moreover, the protein has a preferred low affinity conformation.C.Why does 500 mM imidazole result in the elution of a protein with a 6X-His tag?
- What amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine? In relation to the amino acid in the specificity pocket, which peptide bond is cleaved; C terminal or N terminal? What is this bond’s proximity to the serine in the active site?A) illustrate in molecular detail how hemoglobin's reduced oxygen affinity is caused by protonation of the histidine side chain. b) what is the pKa of the histidine side-chain ionizable group expected to have?In fact, immunoglobulin G consists of two identical copies of the heavy chain and two identical copies of the light chain. However, the early researchers did not know the exact number of chains or how they were arranged. Draw a simple diagram of an alternative quaternary structure for immunoglobulin G, showing how the heavy and light chains might be arranged and connected by disulfide bonds to form a structure with a total molecular mass of 150,000.