Hi, Can someone please answer me questions 8 and 9. Thank you very much!
describe how the steady-state reaction velocity may be de in part (a). n one sentence (or a simple equation sketch if you prefer), termined from your curve(s) 8) a) A bacterial protease cleaves peptide bonds that immediately follow e Glu. To assay th ither Asp or e enzyme's activity, a tripeptide substrate was used, with sequence Ala are performed at 25 C and pH 7, using an enzyme concentration of O 1 d substrate concentration of 1 mM. Since the NMR signal from Tyr in u-Tyr. A micromolar, and the peptide is significantly different from free Tyr, an NMR spcmete monitor the appearance of free tyrosine product. The rate of pr found to be 0.5 mM/sec. r is used to oduct formation was Use the information above to calculate kcat if you can (showing your explain sketch if you prefer. work ). Or briefly why you can't calculate kcat, using only one or two sentences, or perhaps a (b) The experiment is repeated using the same concentration of enzyme, but now with a substrate concentration of 8 mM. The rate of product formation was again found to be 0.5 mM/sec. Use the information given in parts (a) and (b) (the reaction velocity at 2 substrate concentrations) to calculate kcat if you can, or briefly explain why you can't calculate kcat. Show your work. 9) Consider a chemical reaction that converts a reactant (R) to product (P). Draw pair of free energy diagrams that qualitatively illustrate the difference between an endergonic reaction with a ÎG of +5 kJ/mole, and an exergonic reaction with a ÎG of-5 Use the labels "R" and "P" to indicate which parts of the free energy diagram ely. Use a vertical arrow to illustrate the distance on each diagram that represents 5 k]/mole. humotrynsin, trypsin, elastase and thrombin similar? In what
