Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
8th Edition
ISBN: 9780134015187
Author: John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 12.8, Problem 12.1MRP
Interpretation Introduction
Interpretation:
The mechanism of the given reaction has to be explained using curved arrow formalism.
Concept Introduction:
Curved Arrow formalism: The tail of the arrow is placed on the electrons that move. Electrons never flow from atoms which are electron-poor to atoms which are electron-rich, so a curved arrow will never point from an atom with a positive charge to an atom with a negative charge.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
(problem 2.25 textbook, see page 41) Stoichiometry and Incomplete Reactions
For production of penicillin (C16H18O4N2S) using Penicillium mold, glucose (C6H12O6) is used as a substrate and phenylacetic acid (C8H8O2) is added as a precursor. The stoichiometry for overall synthesis is:
1.67 C6H12O6 + 2NH3 + 0.5O2+ H2SO4 + C8H8O2 à C16H18O4N2S + 2CO2 + 9H2O
What is the maximum theoretical yield of penicillin from glucose in g/g?
When results from a particular penicillin fermentation were analyzed, it was found that 24% of the glucose had been used for growth, 70% for cell maintenance activities (such as membrane transport and macromolecule turnover) and only 6% for penicillin synthesis. Calculate the yield of penicillin from glucose in g/g under these conditions.
Batch fermentation under the conditions described in part b) is carried out in a 100-liter Remember that only 6% of the glucose is used for penicillin synthesis. Initially, the tank is filled with nutrient medium…
Problem 3
Is the protonation state of the tripeptide, Glu-Lys-Cys, as drawn below feasible? If so, at what pH? If not,
why not? What is the isoelectric point for this tripeptide?
O OH
SH
*H,N
NH
Practice Problem 25.73
O Get help answering Molecular Drawing questions.
Treatment of a tripeptide with phenyl isothiocyanate yields compound A and a dipeptide. Treatment of the dipeptide with phenyl isothiocyanate yields compound B and glycine. Identify the structure of the
starting tripeptide. Include stereochemistry in your answer. Do NOT explicitly draw any hydrogen atoms in your structure or use abbreviations like OMe, COOH or Ph.
HN-
HN-
Compound A
Compound B
Edit
Chapter 12 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
Ch. 12.2 - Locate and identify the functional groups in (a)...Ch. 12.2 - Draw structures for molecules that fit the...Ch. 12.3 - Prob. 12.3PCh. 12.3 - There are two branched-chain isomers with the...Ch. 12.4 - Draw the following three isomers of C5H12 as...Ch. 12.4 - Prob. 12.6PCh. 12.4 - Prob. 12.7PCh. 12.4 - Draw both condensed and line structures for the...Ch. 12.5 - Which of the following structures represent the...Ch. 12.5 - Are the pairs of compounds shown below the same...
Ch. 12.6 - Identify each carbon in the molecule shown in...Ch. 12.6 - Prob. 12.12PCh. 12.6 - Prob. 12.13PCh. 12.6 - Draw and name alkanes that meet the following...Ch. 12.6 - Prob. 12.15KCPCh. 12.6 - Prob. 12.1CIAPCh. 12.6 - Prob. 12.2CIAPCh. 12.6 - Prob. 12.3CIAPCh. 12.8 - Prob. 12.1MRPCh. 12.8 - Prob. 12.2MRPCh. 12.8 - Prob. 12.16PCh. 12.8 - Write the structures of all singly chlorinated...Ch. 12.10 - Prob. 12.18PCh. 12.10 - Prob. 12.19PCh. 12.10 - What is wrong with the following names? It will be...Ch. 12.10 - Prob. 12.21KCPCh. 12.10 - Prob. 12.4CIAPCh. 12.10 - (a) What common produce items might you see...Ch. 12 - Convert the following models into line drawings...Ch. 12 - Prob. 12.23UKCCh. 12 - Prob. 12.24UKCCh. 12 - Give the IUPAC names for the following...Ch. 12 - Prob. 12.26UKCCh. 12 - What characteristics of carbon make possible the...Ch. 12 - Prob. 12.28APCh. 12 - Prob. 12.29APCh. 12 - Prob. 12.30APCh. 12 - For each of the following, give an example of a...Ch. 12 - Identify the highlighted functional groups in the...Ch. 12 - Identify the functional groups in the following...Ch. 12 - Propose structures for molecules that fit the...Ch. 12 - Prob. 12.35APCh. 12 - What requirement must be met for two compounds to...Ch. 12 - Prob. 12.37APCh. 12 - Prob. 12.38APCh. 12 - Prob. 12.39APCh. 12 - Prob. 12.40APCh. 12 - Give an example of a compound that meets the...Ch. 12 - (a)There are two isomers with the formula C4H10....Ch. 12 - Write condensed structures for the following...Ch. 12 - Prob. 12.44APCh. 12 - Prob. 12.45APCh. 12 - Which of the following pairs of structures are...Ch. 12 - Prob. 12.47APCh. 12 - Prob. 12.48APCh. 12 - Prob. 12.49APCh. 12 - What are the IUPAC names of the following alkanes?Ch. 12 - Prob. 12.51APCh. 12 - Write condensed structures for the following...Ch. 12 - Draw line structures for the following...Ch. 12 - Name the following cycloalkanes:Ch. 12 - Prob. 12.55APCh. 12 - Prob. 12.56APCh. 12 - Prob. 12.57APCh. 12 - Prob. 12.58APCh. 12 - Prob. 12.59APCh. 12 - Prob. 12.60APCh. 12 - Prob. 12.61APCh. 12 - Write the formulas of the four singly chlorinated...Ch. 12 - Write the formulas of the three doubly brominated...Ch. 12 - Identify the indicated functional groups in the...Ch. 12 - The line structure for pregabalin (Lyrica) is...Ch. 12 - Prob. 12.66CPCh. 12 - Prob. 12.67CPCh. 12 - Most lipsticks are about 70% castor oil and wax....Ch. 12 - Prob. 12.69CPCh. 12 - Prob. 12.70CPCh. 12 - Prob. 12.71CPCh. 12 - Which of the following structures represent the...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Problem #2 a) How many ionizable groups does the tyrosine-alanine-isoleucine-glycine tetrapeptide core of ustiloxin B have? ( b) At neutral pH, what fraction of the total concentration of the tetrapeptide is expected to have the R group of the tyrosine residue in its deprotonated, anionic form (assuming that the pK, of the R group is the same as that of the free amino acid)? c) What is the pl of the tetrapeptide (assuming that the pK,'s of the N- and C-termini are also the same as the corresponding functional groups in a free amino acid)?arrow_forwardProblem 1: Calculate the hydrolysis of ATP at pH 7 at 37°C under steady state conditions in which the concentration of ATP, ADP and Pi are maintained at 10-³M, 10 M and 10-2M, respectively. The AG' of hydrolysis of ATP at pH 7 = -32,217 J/mole, R = 8.314 JK ¹mol-¹, T= 273 + 37 K. ATP ADP + Piarrow_forward8arrow_forward
- Study problem 2 4. A coworker has just isolated a copper enzyme that catalyzes the conversion of oil sludge into soluble alcohols in the presence of O₂. There are two Cu atoms per protein, which consists of a single polypeptide chain. As the bioinorganic chemist on the project, you are given unlimited quantities of the protein for the purpose of determining the active site structure. You have at your disposal a number of physical techniques, including NMR and EPR spectrometers, a magnetic susceptometer, a Mössbauer instrument, an X-ray absorption beam line, a UV-VIS spectrophotometer, a Raman spectrometer, a magnetic circular dichroism instrument, but, alas, no X-ray diffractometer. You have time to complete measurements by only three techniques before you have to give a report to your colleague. Describe what measurements you would make, in what order you would make them to get the most out of time, what results you might expect, and how you would use this information to characterize…arrow_forwardQuestion attachedarrow_forwardProblem 3) Take the creation of salt from sodium and molecular chlorine: 2 Na + C12 =2 NaCl A) Write out how the equilibrium constant K will be related to the concentrations of each chemical (as variables, similar to eqn: [H2][H]-2 [H2] = K(t)). [H]2 %3D B) Write out what the equilibrium constant K will be from the quantum concentrations and internal free energy of each molecule (as variables, similar to eqn: log K = log no (H2) – 2 log no (H) - ) %3D C) Find the exact numerical equilibrium constant if the internal free energies are equal to the dissociation energies (FNa = 0, FNaci = -4.26 eV, and Fci = -2.48 e), and the masses are = 7.3 x 10-7 evs2 m2 MNacı = 6.0 × 10-7 eVs2 m2 MNa = 2.3 x 10-7 eVs2 m2 and the temperature Mclz of the system is . A useful constant is T = 300k 0.26 eV. A useful constant is h = 6.58 x 10-16eVs D) Finally, use the equilibrium constant to find how many moles of NaCl will exist in equilibrium with 1.0 mole of Na and 1.0 mole of Cl2.arrow_forward
- PROBLEMS 7.1 The following results were obtained for an enzyme-catalysed reaction Substrate concentration (mmol I'): 5.0 Initial velocity (umol l' min"): 6.67 182 10.0 233 20.0 323 40.0 147 400 Calculate Km and Vma 7.2 Malate dehydrogenase catalyses the reaction: (S)-malate + NAD oxaloacetate + NADH + H The rate of the forward reaction was investigated in the presence of saturating concentrations of malate and a fixed concentration of enzyme. The following results were obtained: Absorbance (at 340 nm) at time t (minutes) [NAD'] (mmol 1") t = 0.5 1.0 1.5 2.0 2.5 3.0 1.5 0.033 0.056 0.079 0.102 0.036 0.063 0.089 0.116 0.040 0.069 0.043 0.075 0.108 0.140 0.047 0.084 0.121 0.158 0.052 0.095 0.137 0.180 0.122 0.138 2.0 0.138 0.150 0.154 2.5 0.099 0.128 0.168 3.33 5.0 0.163 0.175 0.177 0.184 0.192 0.200 10.0 Calculate Km and Vmax -arrow_forwardPROBLEM 2: A biochemist dliscovers and purifies a new enzyme, generating a purification table below The step of protein purification Total Total Specific Total The multi- Total activity yicld (%) cnzyme fold protcin (mg) maltifold activity increase in purification (units) purity Whole-cell lysate 8.4 LO 500 l00 4200 40% ammonium 22.2 95 2.64 9.64 180 3990 sulfate Ion exchange 90.2 251 6.63 68 3787 55.7 Gel filtration 50 5000 to0 119 1.8 11.9 (a) From the information given in the table, calculate the specific activity of the enzyme, total yield (%), multi-fold increase in purity, and total multifold purification after each purification procedure. b) Which of the purification procedures used for the enzyme is most effective (Le., gives the greatest relative increase in purity)? (c) Which step - ion-exchange or gel filtration chromatography - causes the greatest loss of the protein. (d) If you wanted to use only one purification step, which technique would you choose?arrow_forwardProblem 4. Calculate the amount of rice bran (12.5% CP), com (8.5% CP), soybean meal (49% CP) and copra meal (20% CP) in formulating 100 kg diet with 20% CP. Assume that the energy mixture will have a ratio of 2:1 and protein ingredients proportion is 1:3. Show your solution:arrow_forward
- PHBP 211 Sample Problem 2 ● If the half-life for the decomposition of a drug is 4 hours, how long will it take for 225 mg of the drug to decompose by 30%. Assume first order kinetics and constant temperature.arrow_forwardProblem 1. Denitrifying bacteria can substitute NO3 (nitrate) for O2 as the their electron acceptor to oxidize organic compounds and utilize the energy that they conserve from this respiration process to synthesize cell biomass (C5H7O2N). This process can be described by the following balanced reaction, which incorporates respiration of benzoate (C6H5CO0') using NO3 as the electron acceptor plus cell synthesis: 0.0333 C6H5COO' + 0.1096 NO3 + 0.1096 H* ---> 0.01096 C5H¬O2N + 0.045 N2 + 0.1018 CO2 + 0.0333 HCO3 + 0.0528 H2O a.) Determine Y in terms of g cells or VSS/C,H5COO- b.) Determine Y in terms of g cells or VSS/g COD. Recall when converting C,H5COO to COD that the COD concentration does not include the O, required to oxidize NH3. Note also that even though the bacteria are using NO3 instead of O2 to oxidize the C6H5COO', we can still calculate the O2 demand of C6H5COO', by writing a balanced oxidation-reduction using O2 as the electron acceptor.arrow_forwardQuestion attachedarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning