Why is solubility phe > tyr ?
achim at ibex.ca
Thu Jun 6 14:46:43 EST 1996
I have a question concerning the solubilities of the amino acids phenylalanine and
I had posted this message already a few weeks ago, but received no answer, therefore, I am
trying again, and to more Newsgroups.
I am working with an enzyme that accepts phenylalanine (phe) and tyrosine (tyr) as
When I prepared the first time stock solutions I was surprised to notice that phe is
soluble in water at pH 7 +/- 1 pH to approx. 180 mM, while with tyr I can prepare at the
same conditions only a 10 mM solution.
Tyr differs from phe only in an additional hydroxyl-group.
I had always assumed an increase in polarity would also make a substance more water
Can anybody explain to me, why the p-OH group in tyrosine has such a strong effect on the
solubility of the amino acid, nin effect decreasing it almost to 1/20 of phe.
Is this only valid for the free enzyme, or would this also be the case for the amino acid
side-chains in proteins? Does this mean, phe-side-chains have a more hydrophilic
character than tyr¹s in proteins?
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