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Serine (symbol Ser or S) [3] [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α- amino group (which is in the protonated − NH + 3 form under biological conditions), a carboxyl group (which is in the deprotonated − COO −
The polar, uncharged amino acids serine (Ser, S), threonine (Thr, T), ... and some amino acids (in particular, with nonpolar side chains) can be isolated by ...
Valine (symbol Val or V) [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH 3 + form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain isopropyl group, making it a non-polar aliphatic amino acid.
^a EINECS for Serine ^a CID 617 from PubChem ^a CID 5951 from PubChem This page was last edited on 12 April 2023, at 11:39 (UTC). Text is available under the ...
Their hydrophobic tendency was equivalent to that of known nonpolar amino acids such as methionine and tyrosine (tyrosine is polar aromatic but also hydrophobic [29]), those of which were much greater than that of known polar amino acids such as serine and threonine. [30]
It is a conditionally essential amino acid with a polar side group. The word "tyrosine" is from the Greek tyrós, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. [3] [4] It is called tyrosyl when referred to as a functional group or side chain.
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When comparing a polar and nonpolar molecule with similar molar masses, the polar molecule in general has a higher boiling point, because the dipole–dipole interaction between polar molecules results in stronger intermolecular attractions. One common form of polar interaction is the hydrogen bond, which is also