Chapter 32: Problem 736
Of what importance are proteins to biological svstems?
Chapter 32: Problem 736
Of what importance are proteins to biological svstems?
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Get started for freeHemoglobin, the protein responsible for carrying oxygen from the lungs to the body tissues, contains \(0.355\) per cent iron. Hydrolysis of \(100 \mathrm{~g}\) of hemoglobin gives \(1.48 \mathrm{~g}\) of tryptphan; calculate the minimum molecular weight of hemoglobin which is consistent with these results.
Give formulas for compounds \(\mathrm{A}-\mathrm{G}\), and tell what is happening in each reaction. polystyrene \(+\mathrm{CH}_{3} \mathrm{OCH}_{2} \mathrm{Cl}(\mathrm{SnCl} 4) \rightarrow \mathrm{A}+\mathrm{CH}_{3} \mathrm{OH}\) \(\mathrm{A}+\mathrm{C}_{6} \mathrm{H}_{5} \mathrm{CH}_{2} \mathrm{OCONHCH}_{2} \mathrm{COO}^{-+} \mathrm{NHEt}_{3} \rightarrow \mathrm{B}+\mathrm{Et}_{3} \mathrm{NHCl}\) \(\mathrm{B}+\) dil. \(\mathrm{HBr} \rightarrow \mathrm{C}+\mathrm{C}_{6} \mathrm{H}_{5} \mathrm{CH}_{2} \mathrm{Br}+\mathrm{CO}_{2}\) \(\mathrm{C}+\) carbobenzoxyalanylchloride \(\rightarrow \mathrm{D}\) \(\mathrm{D}+\) dil \(\mathrm{HBr} \rightarrow \mathrm{E}+\mathrm{C}_{6} \mathrm{H}_{5} \mathrm{CH}_{2} \mathrm{Br}+\mathrm{CO}_{2}\) \(\mathrm{E}+\mathrm{HBr}\left(\mathrm{CF}_{3} \mathrm{COOH}\right)^{\rightarrow} \mathrm{F}\left(\mathrm{C}_{6} \mathrm{H}_{5} \mathrm{CH}_{2} \mathrm{Br}\right)^{\rightarrow}+\mathrm{G}\)
Explain how the conjugate base of thiamine might react with pyruvic acid to produce an intermediate which could easily decarboxylate. Complete the reaction sequence leading to the formation of acetoin.
Many years before the Hofmann degradation of optically active a-phenylpropionamide was studied, the following observations were made: when the cyclopentane derivative, \(\mathrm{I}\), in which the \(-\mathrm{COOH}\) and \(-\mathrm{CONH}_{2}\) groups are cis to each other, was treated with hypobromite, compound II was obtained; compound II could be converted by heat into the amide III (called a lactam). What do these results show about the mechanism of the rearrangement? (Use models.)
The complete structure of Gramicidin \(\mathrm{S}\), a polypeptide with antibiotic properties, has been worked out as follows: (a) Analysis of the hydrolysis products gave an empirical formula of Leu, Orn, Phe, Pro, Val. (Ornithine, Orn, is a rare amino acid of formula \(\left.{ }^{+} \mathrm{H}_{3} \mathrm{NCH}_{2} \mathrm{CH}_{2} \mathrm{CH}_{2} \mathrm{CH}\left(\mathrm{NH}_{2}\right) \mathrm{COO}^{-} .\right)\) It is interesting that the phenylalanine has the unusual D-configuration. Measurement of the molecular weight gave an approximate value of \(1300 .\) On this basis, what is the molecular formula of Gramicidin \(\mathrm{S} ?\) (b) Analysis for the C-terminal residue was negative; analysis for the N-terminal residue using DNFB yielded only DNP-NHCH \(_{2} \mathrm{CH}_{2} \mathrm{CH}_{2} \mathrm{CH}\left(\mathrm{N}^{+} \mathrm{H}_{3}\right) \mathrm{COO}^{-}\). What structural feature must the peptide chain possess? (c) Partial hydrolysis of Gramicidin \(\mathrm{S}\) gave the following di- and tripeptides: Leu.Phe Phe.Pro Phe.Pro.Val Val.Orn.Leu \(\begin{array}{lll}\text { Orn.Leu } & \text { Val.Orn } & \text { Pro. Val.Orn }\end{array}\) What is the structure of Gramicidin \(\mathrm{S} ?\)
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