Concept explainers
Cisplatin [Pt(NH3)2Cl2], a compound used in cancer treatment, is prepared by reaction of ammonia with potassium tetrachloroplatinate:
- (a) How many grams of NH3 are needed to react with 55.8 g of K2PtCl4?
- (b) How many grams of cisplatin are formed from 55.8 g of K2PtCl4 if the percent yield for the reaction is 95%?
Want to see the full answer?
Check out a sample textbook solutionChapter 6 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
- H OH CH2OH D H ОН H الحزن ОН CH2OH ОН H ОН I Which of the following statements correctly describes this structure? (A) The monomer units are bonded by beta 1-2 glycosidic linkage. B The monomer units are bonded by alpha 1-2 glycosidic linkage. The monomer units are bonded by alpha 1-4 glycosidic linkage. The monomer units are bonded by beta 1-4 glycosidic linkage. H CH2OH H ОН H ОН H ОНarrow_forwardAt equilibrium, D-galactose exists almost exclusively in its α and β pyranose forms. Aqueous solutions are freshly prepared for the α and β forms, both at the same concentration and temperature. The solution of the α form rotatesplane-polarized light +150.7°, whereas the solution of the β form rotates the light +52.8°. Over time, both solutions have the same measured rotation of +80.2°. How much of the equilibrated solution does each form account for?arrow_forwardA sample (660 mg) of a (homo)oligomeric protein of molecular weight of 132,000 Da was treated with an excess of 2,4-dinitro-fluorobenzene until the reaction was complete. The peptide bonds were then completely hydrolyzed by heating with 6 M hydrochloric acid. The hydrolysate was found to contain 5.5 mg of the following compound. NO2 O2N- NH НООС 2,4-Dinitrophenyl derivatives of the amino groups of other amino acids were not found. a). How many polypeptide chains are there in this protein? Show your work. b). Assuming that each of the subunit contains entirely a-helices, how many a-helical turns would there be, approximately, in each of the subunit? "For a protein of typical composition, average amino acid residue mass is ca. 110 Da."arrow_forward
- Using the generic structure shown, indicate what the substituents are for the structure of finerenone (R1, R2, R3, for Ar indicate R6, R8, R9, R10, for D indicate R4). R1 R2 R3 = For Ar: R6 R8 = R9 = R10 = For D: R4= Finerenone: H₂N HC Generic formula: H₂N 230 R+ 'R'. R$ ofarrow_forwardTitration of alanine by a strong base, for example NaOH, reveals two pk's. Which is the titration reaction occurring at pK1 (pK1 = %3D 2.34)? O-NH2 + COH →-NH + H2O O-COOH + OH →-CO + H20 -COOH + -NH2 → -COO" + -NH2+ -CoO +-NH2* → -COOH +-NH2 O -NH3* + OH →-NH2 + H2Oarrow_forwardWhat is the net average charge on the predominant form of lysine at pH values of (a) 2.0, (b) 5.0and (c) 7.0?arrow_forward
- Assume that you are conducting a chain-addition polymerization using 5.47 grams of monomer (MW= 68.7g/mol) and 118 mg of initiator (MW= 190.5 g/mol). What is the expected number of repeat units (n) per chain? Report your answer to the nearest whole number (i.e., an answer of 112.3 should be reported as 112).arrow_forwardA solution contains a mixture of four proteins: urease, ovalbumin, lysozyme, and alkaline phosphatase. The proteins have the following properties. Molecular weight (Daltons) Protein pl Urease 483,000 5.0 Ovalbumin 45,000 4.6 Lysozyme 86,000 11.0 Alkaline 86,000 4.6 Phosphatase Based on the information provided, what type of chromatography (gel permeation or ion exchange) could be used to separate: a) Lysozyme from Alkaline Phosphatase. Briefly explain your answer. b) Ovalbumin from Alkaline Phosphatase. Briefly explain your answer. c) Which of the four proteins would be bound to a cation exchanger equilibrated at pH 5? d) Briefly explain your answer to part c).arrow_forwardHemoglobin is considered to be a tetrameric complex with a 64 kDa (α β)2. When attempting to purify hemoglobin, we must first purify the α and β monomers (about 16 kDa each) to prepare the tetramer. This is formed from the dimer intermediate: 2 α + 2 β -> 2 αβ -> (α β)2. The graph given represents a size-exclusion chromatogram after the refolding of the hemoglobin tetramer Using the size-exclusion chromatogram given, 1. Draw an SDS-Page Gel with a reducing agent such as BME using the three peaks listed on the graph.arrow_forward
- The following proteins were separated by SDS-PAGE in the presence of mercaptoethanol. Sketch the relative positions of the various polypeptides on the gel. Label the positive and negative ends of the gel.Protein A: 40 kDa single polypeptideProtein B: 80 kDa protein, made up of two subunits of molecular weight 20 kDa and 60 kDa, held together by noncovalent interactionsProtein C: 200 kDa protein, made up of four identical subunits (50 kDa each) linked together by disulfide bondsarrow_forwardIn principle, there are many different, chemically diverse ways in which small molecules can be linked to form polymers. For example, the small molecule ethene (CH2=CH2) is used commercially to make the plastic polyethylene (...–CH2–CH2– CH2–CH2–CH2–...). The individual subunits of the three major classes of biological macromolecules, however, are all linked by similar reaction mechanisms, i.e., by condensation reactions that eliminate water. Can you think of any benefits that this chemistry offers and why it might have been selected in evolution?arrow_forward(A) What are Waxes? Draw the structure of wax, which is made up of palmitic acid (16:0) and a saturated 18-carbon alcohol. (В) Consider the structure of menthol. How many isoprene units are present in menthol? (C) What type of isoprene linkage (head-to-tail or tail-to-tail) is present in menthol? Identify the isoprene linkage in the following structure of menthol and indicate by a circle. Menthol =arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON