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- Some of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a side chain for acid-base catalysis at physiological pH (assume pK of each amino acid is equal to pK value for the free amino acid in solution). Explain for each amino acid how and why each would or would not provide the side chain residue to support acid-base catalysis at physiological pH.. (a) Explain the biochemical basis for the fact that one can synchro- nize cell populations þy treating them with deoxythymidine. (b) Explain the apparent paradox that dATP at low concentrations is an activator of ribonucleotide reductase, whereas at higher concen- trations it becomes inhibitory.. Provide an explanation for the fact that a-D-mannose is more stable than B-D-mannose, whereas the opposite is true for glucose.
- a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).Briefly describe each of the following possible posttranslational protein modifications. Give an example of each. Cross-linkage glycosylation and phosphorylation cleavage assembly into polymeric proteins (> 1 polypeptide)Equilibrium constants are always dependent upon temperature. In determining equilibrium constants for biochemical reactions the equilibrium constant also depends upon ion concentration and proton concentration. Write down an equation in differential form that describe the dependence of an equilibrium constant K for a protein binding to DNA, where the equilibrium constant, K is a function of Temperature, [NaCI], and [H*], i.e. dK(T, [NaCl], [H*]).
- Provide a simple sketch of the covalent intermediate likely to form between active site serine residue and diphenylcarbamyl chloride. Is DPCC more likely to covalently bind to serine, aspartate, or histidine?Consider a protein with two surface-exposed histidine residues: HisA is a “typical” histidine residue with a pKa = 6.2 HisB is involved in a stabilizing interaction (His-NH+ ..... -O2C-Glu) with a neighboring glutamic acid residue. For HisB, the Gibbs free energy of deprotonation at pH = 7.0 and T = 293K is ΔG'o = +15 kj mol-1. If you had a solution, at pH = 7.0 and T = 293K, containing this protein: a) What fraction of HisA residues are protonated? b) What fraction of HisB residues are protonated? c) What is the pKa of HisB?Refer to the molecular structure of Molecule 1 (attached image). This molecule forms a dimer via pi interactions, resulting to effective molecular stacking. If the molecule can inhibit toxic effects at 0.5mM against gastric carcinoma cells, does it mean that the dimer of this nucleoside analogue will exhibit an IC50 of about 0.25mM?
- Will rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine A) I, II, III B) I, II C) I D) II E) I, IIIWhen performing his experiments on protein refolding, Christian Anfinsen obtained a quite different result when reduced ribonuclease was reoxidized while it was still in 8 M urea and the preparation was then dialyzed to remove the urea. Ribonuclease reoxidized in this way had only 1% of the enzymatic activity of the native protein. Why were the outcomes so different when reduced ribonuclease was reoxidized in the presence and absence of urea?It is important to note that galactose is an important component of glyco- proteins. What is the effect on glycoprotein synthesis in case of galactosemic patients who are not given galactose in their diet? Explain this observation.