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2. Theanine - Wikipedia

   en.wikipedia.org/wiki/Theanine

   The name theanine usually refers to the enantiomer L-theanine, which is the form found in tea leaves from which it is extracted as a powder. [4] [6] The right-handed enantiomer, D-theanine, is less-studied. Theanine is sold as a dietary supplement and is considered to be safe at doses up to 250 milligrams (mg) by the US Food and Drug ...

3. What You Should Know Before Taking a L-Theanine ... - AOL

   www.aol.com/know-taking-l-theanine-supplement...

   Tea's combination of caffeine and L-theanine can give you a calm yet alert mental state that could help boost productivity and effectiveness,” Ingram explains, citing a 2021 study on caffeine ...

4. The Exact Right Time to Take L-Theanine - AOL

   www.aol.com/lifestyle/exact-time-l-theanine...

   L-theanine is an amino acid, a.k.a. a molecule that helps build protein in the body. It’s often talked about as being found in green tea, but it's also present in other herbal brews such as ...

5. Tryptophan - Wikipedia

   en.wikipedia.org/wiki/Tryptophan

   Tryptophan (symbol Trp or W) [3] is an α-amino acid that is used in the biosynthesis of proteins.Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent.

6. 5-Hydroxytryptophan - Wikipedia

   en.wikipedia.org/wiki/5-Hydroxytryptophan

   5-HTP is produced from the amino acid tryptophan through the action of the enzyme tryptophan hydroxylase. Tryptophan hydroxylase is one of the biopterin-dependent aromatic amino acid hydroxylases. Production of 5-HTP is the rate-limiting step in 5-HT (serotonin) synthesis. 5-HTP is normally rapidly converted to 5-HT by amino acid decarboxylase. [1]

7. trp operon - Wikipedia

   en.wikipedia.org/wiki/Trp_operon

   Structure of the trp operon. The trp operon is a group of genes that are transcribed together, encoding the enzymes that produce the amino acid tryptophan in bacteria. The trp operon was first characterized in Escherichia coli, and it has since been discovered in many other bacteria. [1]

8. Tryptophan (data page) - Wikipedia

   en.wikipedia.org/wiki/Tryptophan_(data_page)

   Download QR code; Print/export Download as PDF; Printable version; In other projects ... ^a EINECS for Tryptophan ^a CID 9060 from PubChem ^a CID 6305 from PubChem

9. Fluorescence spectroscopy - Wikipedia

   en.wikipedia.org/wiki/Fluorescence_spectroscopy

   In addition, tryptophan is a relatively rare amino acid; many proteins contain only one or a few tryptophan residues. Therefore, tryptophan fluorescence can be a very sensitive measurement of the conformational state of individual tryptophan residues. The advantage compared to extrinsic probes is that the protein itself is not changed.