Chapter 24: Problem 94
Can a DNA strand bind to a complementary RNA strand? Explain.
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Chapter 24: Problem 94
Can a DNA strand bind to a complementary RNA strand? Explain.
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Are carbon monoxide or ammonia considered organic molecules? Why or why not?
The protein ribonuclease A in its native, or most stable, form is folded into a compact globular shape:(a) Does the native form have a lower or higher free energy than the denatured form, in which the protein is an extended chain? (b) What is the sign of the entropy change in going from the denatured to the folded form? (c) In the native form, the molecule has four \(-\mathrm{S}-\mathrm{S}-\) bonds that bridge parts of the chain. What effect do you predict these four linkages to have on the free energy and entropy of the native form relative to the free energy and entropy of a hypothetical folded structure that does not have any \(-\mathrm{S}-\mathrm{S}-\) linkages? Explain. \((\mathrm{d})\) A gentle reducing agent converts the four \(-\mathrm{S}-\mathrm{S}-\) linkages in ribonuclease \(A\) to eight \(-S-H\) bonds. What effect do you predict this conversion to have on the tertiary structure and entropy of the protein? (e) Which amino acid must be present for \(-\mathrm{SH}\) bonds to exist in ribonuclease \(\mathrm{A}\) ?
What are the approximate bond angles (a) about carbon in an alkane, (b) about a doubly bonded carbon atom in an alkene, (c) about a triply bonded carbon atom in an alkyne?
Write the condensed structural formula for each of the following compounds: (a) 2 -pentanol, (b) 1,2 -propanediol, (c) ethyl acetate, (d) diphenyl ketone, (e) methyl ethyl ether.
(a) Describe the primary, secondary, and tertiary structures of proteins. (b) Quaternary structures of proteins arise if two or more smaller polypeptides or proteins associate with each other to make an overall much larger protein structure. The association is due to the same hydrogen bonding, electrostatic, and dispersion forces we have seen before. Hemoglobin, the protein used to transport oxygen molecules in our blood, is an example of a protein that has quaternary structure. Hemoglobin is a tetramer; it is made of four smaller polypeptides, two "alphas" and two "betas." (These names do not imply anything about the number of alpha-helices or beta sheets in the individual polypeptides.) What kind of experiments would provide sound evidence that hemoglobin exists as a tetramer and not as one enormous polypeptide chain? You may need to look into the chemical literature to discover techniques that chemists and biochemists use to make these decisions.
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