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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. 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 ...

4. 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 ...

5. 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).

6. 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.

7. Alpha helix - Wikipedia

   en.wikipedia.org/wiki/Alpha_helix

   The alpha helix is also commonly called a: Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure); 3.6 13-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen)

8. 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 ...

9. Amino acid synthesis - Wikipedia

   en.wikipedia.org/wiki/Amino_acid_synthesis

   Amino acid biosynthesis is the set of biochemical processes (metabolic pathways) by which the amino acids are produced. The substrates for these processes are various compounds in the organism 's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids.