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- Biomaterial question: Give a brief and clear answer, please Sketch a typical stress-strain curve for three major types of biomaterials. Describe Young’s modulus and write Hooke’s Law. What are the time-dependent properties of materials? Explain briefly.Question: Assume two Silver/Silver-Chloride electrodes are interfacing with human tissue using the Direct contact and Gel-filled contact approaches. In one paragraph, describe which method is the better technique to reduce motion artifacts and explain why.Biomaterial question: Give a brief and clear answer, please a. Briefly describe the structural differences between the three major types of biomaterials, including their chemical structure, bonding characteristics, crystal structures, etc. b. Explain briefly the working principle and the information provided by the spectroscopic and chromatographic characterization techniques . Give an example to each of them.
- MATHEMATICAL If a reaction can be written AB, and the G is 20kJmol1, what would the substrate/product ratio have to be for the reaction to be thermodynamically favorable?Time remaining: 00:08:55 Chemistry Consider a peptide with the following amino acid sequence: H2N-ASENHLDGCPYTKSRG-COOH Analyze the predominate protonation state and thus dominate charge (+1, 0, -1) of the residues in this peptide at pH 3, 6, and 10 by filling in the table below, identifying the relevant pKa appropriate for each residue. (Note that choice of pKa and its. application will be graded independently; e.g., if you can choose the wrong pKa but apply it correctly, you will lose points only for the pKa.) AA Residue pKa Charge pH 3 Charge pH 6 Charge pH 10 A S E N H L D G C P Y T K S R G[Ten - Biomolecules] INSTRUCTIONS — Answer the following multiple-choice questions and EXPLAIN in 3-5 sentences why you chose that answer. — Answer properly Questions; Thomas was purifying an enzyme from a homogenate of muscle cells. He went through seven steps of purification and found that the enzyme activity was the same as the homogenate value. On the eighth step, when the protein washighly pure, the enzyme activity rose to five times that of the homogenate value. Can you suggest a possible reason? A. the homogenate assay was wrong B. step eight has co-purified an activator of the enzyme. C. the enzyme has an inhibitor present in the muscle cell homogenate D. the temperature at step eight was just right for the enzyme activity.
- Exercise 5-9 Phenylalanine deaminase Phenylalanine deaminase positive bacteria can remove the amine functional group from the amino acid and the amine group is released as ammonia waste. Phenylpyruvic acid is also produced by this reaction. What can phenylalanine deaminase positive bacteria do with phenylpyruvic acid?MATHEMATICAL What is the ratio of HEPES/HEPES-H+ in a HEPES buffer at pH 7.9?student question 1. How do both Hemoglobin and S-adenosylmethionine synthetase form hydrophobic pockets? explain in detail. 2. how does the structure of S-adenosylmethionine synthetase make it resistant to heat denaturation and why, explain in detail
- 20. The dissociation constant of protein Z for ligand Y is: 10 micromolar. What fraction of the ligand is bound at ligand concentration = 5 micromolar?MATHEMATICAL If you mix equal volumes of 0.1 M HCl and 0.20 M TRIS (free amine form; see Table 2.8), is the resulting solution a buffer? Why or why not?MATHEMATICAL What is the [CH3COO]/[CH3COOH] ratio in an acetate buffer at pH 5.00?
