1 What is the dominant biochemical activity or molecular interaction that your protein is predicted to carry out? Which sites on the protein contribute to the process directly? Which sites contribute indirectly? protein = amyloid-beta precursor
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What is the dominant biochemical activity or molecular interaction that your protein is predicted to carry out? Which sites on the protein contribute to the process directly? Which sites contribute indirectly?
protein = amyloid-beta precursor
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Solved in 2 steps
- 1. In a protein, why does when Ala is replaced with Ile, it loses its activity but when Lys is replaced by Arg and Leu to Ile, it only has little effect on protein structure and function? Explain. 2. Why do proteins cannot be denatured reversibly when they are chemically altered to change the chemical composition of certain side chains? Explain.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?C.Why does 500 mM imidazole result in the elution of a protein with a 6X-His tag?
- What property enables the residues of the amino acids serine, threonine, and tyrosine to be phosphorylated? They are polar. They are non-polar. They contain a hydroxyl group. They occur more frequently in the amino acid sequence of signaling proteins.Figure 16.13 An increase in phosphorylation levels of elF-2 has been observed in patients with neurodegenerative diseases such as Alzheimer’s, Parkinson's, and Huntington's. What impact do you think this might have on protein synthesis?Which of the following analogies best describes the induced-fit model of enzyme-substrate binding? a hug between two people a key fitting into a lock a square peg fitting through the square bole and a round peg fitting through the round hole of a children’s toy the fitting together of two jigsaw puzzle pieces
- Describe the differences in the four protein structures.With regard to enzymes, why are vitamins necessary for good health? Give examples.2 A biomolecule has a K_d of 1.6mM. A mutated-version of the same biomoleucel was bound by ligan by THIRTY-FIVE-PERCENT, Ligand=1mM. Find the Kd of mutated protein in mM? Does your result show a disruption of binding of biomoilecule(protein)? Why or why not?
- Can the same pepptide be used in multiple different proteins? yes or no, explain.q41 please calculate the unknown concentration of the protein D wih an absorbance value of A412 given the standard curve indicated in the table. write your answers in numbers only with 2 decimals. protein concentration (ug/ml) absorbance 0 0.000 0.02 0.161 0.04 0.284 0.06 0.438 0.08 0.572 0.10 0.7622. Many types of protein–glycan interactions are low affinity, and in some cases high avidity is achieved by clustering receptors and ligands. What are the advantages and disadvantages of achieving high-affinity interactions through multivalency?
