a)True or false: One single hydrogen bond can make the difference between a prot

Question

a)True or false: One single hydrogen bond can make the difference between a protein folding and not folding.
b)List three features that the strongest hydrogen bonds share.
c)Is hydrogen bonding a driving force for protein folding? Why or why not?
d)Are hydrophobic interactions true bonds? Why or why not?
e)Which amino acids can be involved in p-cation interactions?
f)What is the equation for electrostatic interaction energy?
g)Which amino acid can form a covalent bond when near another copy of itself?

Explanation / Answer

a.) True, a single hydrogen bond can indeed prevent a protein from folding; depending on where that bond is and where the protein tries to fold. for instance if there is a hydrogen bond on the previous amino acid, the next couple generally cant fold until further down the molecule. However, the hydrogen bond will break if the protein is more stable overall without it, and it will continue to fold. So... yes it can prevent sections from folding, but preventing an entire protein from folding with one hydrogen bond is a long stretch. b.) The strongest hydrogen bonds will have a hydrogen bond acceptor, and a donor. They will have linear symmetry, and will have a shorter bond length. If this question is a homework assignment you should really look directly in the book, or your notes because it seems like the person that assigned this question has three particular answers in mind. Basically the 3 I gave come from the fact that all hydrogen bonds require a donor and acceptor, the linear symmetry generally implies that there is less interference from other functional groups, and the shorter bond length is just a general fact about chemical bonds... the stronger they are the shorter they are. c.) Hydrogen bonding is by far the most influential force in protein folding. The strength of the numerous hydrogen bonds across a single protein can be massive. This is because hydrogen bonds are a result of attractive interactions between an electronegative ion and a hydrogen atom; both of which are numerous in proteins. So basically when folding the protein is more stable, or it has a lower probability to change its form, when its being held by a hydrogen bond. So as the protein folds, the hydrogen bonds form between the carboxylic acid end of one amino acid and almost any hydrogen atom on another. d.) Hydrophobic interactions are not considered bonds because they are merely the grouping of like molecules. Think of when you drop oil in water... the hydrophobic oil does not dissolve and it clumps together into bubbles... That's exactly what's happening here but on a much smaller scale and slightly more complicated. In this example all of the "oil" molecules are attached to a chain, and because they are all being pushed out of the water and group together.

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