LinkClick - Name: Chem 464 Biochemistry Multiple choice (4...

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N a m e : Chem 464 Biochemistry Multiple choice (4 points apiece): 1. A true statement about hydrophobic interactions is that they: A) are the driving force in the formation of micelles of amphipathic compounds in water. B) do not contribute to the structure of water-soluble proteins. C) have bonding energies of approximately 20–40 Kjoule per mole. D) involve the ability of water to denature proteins. E) primarily involve the effect of polar solutes on the entropy of aqueous systems. 2. In which reaction below does water not participate as a reactant (rather than as a product)? A) Conversion of an acid anhydride to two acids. B) Conversion of an ester to an acid and an alcohol. C) Conversion of ATP to ADP. D) Photosynthesis E) Production of gaseous carbon dioxide from bicarbonate. 3. Of the 20 standard amino acids, only ___________ is not optically active. The reason is that its side chain ___________. A) alanine; is a simple methyl group B) glycine; is a hydrogen atom C) glycine; is unbranched D) lysine; contains only nitrogen E) proline; forms a covalent bond with the amino group 2a 4. The uncommon amino acid selenocysteine has an R group with the structure —CH —SeH (p K . 5). In an aqueous solution, pH = 7.0, selenocysteine would: A) be a fully ionized zwitterion with no net charge . The above answer is the one given in the text. I think it is wrong. If you had this question wrong, and you can tell me what is wrong with their answer I will give you 4 points, but you have to promise not to tell anybody else! B) be found in proteins as D-selenocysteine. C) never be found in a protein. D) be nonionic. E) not be optically active. 5. In a mixture of the five proteins listed below, which should elute second in size-exclusion (gel- filtration) chromatography?
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This note was uploaded on 10/17/2011 for the course CHEM 653 taught by Professor Wei, robert during the Spring '11 term at Cleveland State.

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LinkClick - Name: Chem 464 Biochemistry Multiple choice (4...

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