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2. Lysine - Wikipedia

   en.wikipedia.org/wiki/Lysine

   Lysine (symbol Lys or K) [2] is an α-amino acid that is a precursor to many proteins.It contains an α-amino group (which is in the protonated −NH + 3 form when dissolved in water), an α-carboxylic acid group (which is in the deprotonated −COO − form when dissolved in water), and a side chain lysyl ((CH 2) 4 NH 2), classifying it as a basic, charged (at physiological pH), aliphatic ...

3. Salt bridge (protein and supramolecular) - Wikipedia

   en.wikipedia.org/wiki/Salt_bridge_(protein_and...

   Salt bridge (protein and supramolecular) Figure 1. Example of salt bridge between amino acids glutamic acid and lysine demonstrating electrostatic interaction and hydrogen bonding. In chemistry, a salt bridge is a combination of two non-covalent interactions: hydrogen bonding and ionic bonding (Figure 1).

4. Amino acid - Wikipedia

   en.wikipedia.org/wiki/Amino_acid

   Structure of a typical L-alpha-amino acid in the "neutral" form. Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2] Only these 22 appear in the genetic code of life ...

5. α-Aminoadipate pathway - Wikipedia

   en.wikipedia.org/wiki/Α-aminoadipate_pathway

   The amino acid L-lysine. The α-aminoadipate pathway is a biochemical pathway for the synthesis of the amino acid L-lysine.In the eukaryotes, this pathway is unique to several species of yeast, higher fungi (containing chitin in their cell walls), and the euglenids.

6. Active site - Wikipedia

   en.wikipedia.org/wiki/Active_site

   The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site. Although the active site occupies only ~10–20% of the volume of an enzyme, [ 1 ] : 19 it is the most important part as it directly catalyzes the chemical ...

7. Proline - Wikipedia

   en.wikipedia.org/wiki/Proline

   Furthermore, proline is rarely found in α and β structures as it would reduce the stability of such structures, because its side chain α-nitrogen can only form one nitrogen bond. Additionally, proline is the only amino acid that does not form a red-purple colour when developed by spraying with ninhydrin for uses in chromatography. Proline ...

8. Alpha helix - Wikipedia

   en.wikipedia.org/wiki/Alpha_helix

   An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of local structure, and it is the local structure that is most easily predicted from a sequence of amino ...

9. Lysin - Wikipedia

   en.wikipedia.org/wiki/Lysin

   N-acetylmuramoyl-L-alanine amidase (T7-like, EC 3.5.1.28) γ-D-glutaminyl-L-lysine endopeptidase (EC 3.4.14.13) Peptidoglycan consists of cross-linked amino acids and sugars which form alternating amino sugars: N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM). Endo-β-N-acetylglucosaminidase lysins cleave NAGs while N-acetylmuramidase ...