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Chapter 3 Answers
1. Because secondary bonds are significantly weaker than covalent bonds, you could
distinguish between these possibilities by assessing the overall stability of the protein or
protein complex. Heating the enzyme, for example, would likely be sufficient to separate
distinct polypeptide chains, but would not be enough to break apart a single chain.
2. Because covalent bonds are stronger, the length of the bonds is much shorter than it is
with weak bonds. Also, covalent bonds are more constrained than weak bonds in several
respects. For example, covalent bonds involving a double or triple bond have no freedom of
rotation, in contrast with weak bonds, which are not limited by their relative orientation. In
addition, the angle between any two covalent bonds is fixed, in contrast to the angle between
any two weak bonds. Finally, a given atom can only bond with a very small number of other
atoms (determined by its valence), whereas a weak bond has more flexibility in this regard.
Because secondary bonds are generally too weak to support a stable interaction
between molecules by themselves, stability must come from a collection of multiple wea
bonds acting together. The flexibility of weak bonds can help in this regard, because it
facilitates the formation of these multiple weak interactions. For example, when two proteins
bind to each other, numerous secondary bonds are formed between the exposed molecular
groups of each of the proteins. If each of these bonds were subject to the same rigid
constraints of covalent bonds, the number of possible weak interactions would be limited, and
the demands placed on the precise structure of each protein would be that much greater.
3. Beyond the obvious importance of strong (covalent) bonds in maintaining the primary
structure of polymerase, other enzymes involved in DNA replication, and the DNA strands
themselves, strong bonds are also important for providing the
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