User:Abbey311/sandbox
Amino Acid Template
Alanine (abbreviated as Ala or A; encoded by the codons GCU, GCC, GCA, and GCG) is an ɑ-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated -+NH3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated –COO- form under biological conditions), and a side chain methyl group, classifying it as a nonpolar (at physiological pH), aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it.
L-Alanine is second only to leucine in rate of occurrence, accounting for 7.8% of the primary structure in a sample of 1,150 proteins.[2] The right-handed form, D-Alanine occurs in bacterial cell walls and in some peptide antibiotics.
![](http://upload.wikimedia.org/wikipedia/commons/8/8b/Alanine_at_physiological_pH.png)
Glutamic acid (abbreviated as Glu or E; encoded by the codons GAA or GAG) is an ɑ-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated -+NH3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated –COO- form under biological conditions), and a side chain carboxylic acid, classifying it as a polar negatively charged (at physiological pH), aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it.
In neuroscience, its carboxylate anion glutamate is an important excitatory neurotransmitter that plays the principal role in neural activation.[4]
![](http://upload.wikimedia.org/wikipedia/commons/thumb/c/cb/Glutamic_Acid_at_physiological_pH.png/220px-Glutamic_Acid_at_physiological_pH.png)
![](http://upload.wikimedia.org/wikipedia/commons/thumb/b/b2/Glutamic_Non-ionic.png/220px-Glutamic_Non-ionic.png)
References
[1] Enzymes
Intro
Being bold is important on Wikipedia. <ref> https://wiki.riteme.site/wiki/Wikipedia:Be_bold <ref>
![](http://upload.wikimedia.org/wikipedia/commons/thumb/c/cf/0303_Lipid_Bilayer_With_Various_Components.jpg/220px-0303_Lipid_Bilayer_With_Various_Components.jpg)
Lipid-Anchored Proteins
[edit]![](http://upload.wikimedia.org/wikipedia/commons/thumb/e/ee/CellMembraneDrawing.jpg/220px-CellMembraneDrawing.jpg)
Notes
[edit]- ^ Dai, Han (22 October 2010). "SIRT1 activation by small molecules: kinetic and biophysical evidence for direct interaction of enzyme and activator". J Biol Chem. 285 (43): 32695–32703. doi:10.1074/jbc.M110.133892. PMID 20702418. Retrieved 20 October 2015.
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: CS1 maint: unflagged free DOI (link)
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