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stratz
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Our text says that ionic bonds are much weaker in aqueous solutions than covalent bonds, due to the dissociative properties of most ionic compounds in water. I read elsewhere though, that in general, ionic bonds are stronger due to the increased polarity.
So, in protein folding, when different chains interact, would a lot of polar bonds in the side chains of amino acids result in a tighter, more compact protein structure, or a looser structure?
So, in protein folding, when different chains interact, would a lot of polar bonds in the side chains of amino acids result in a tighter, more compact protein structure, or a looser structure?