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  2. Proline - Wikipedia

    en.wikipedia.org/wiki/Proline

    The "side chain" from the α carbon connects to the nitrogen forming a pyrrolidine loop, classifying it as a aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate. It is encoded by all the codons starting with CC (CCU, CCC, CCA, and CCG).

  3. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    For amino acids with charged side chains, the pK a of the side chain is involved. Thus for aspartate or glutamate with negative side chains, the terminal amino group is essentially entirely in the charged form −NH + 3 , but this positive charge needs to be balanced by the state with just one C-terminal carboxylate group is negatively charged.

  4. Stable isotope composition of amino acids - Wikipedia

    en.wikipedia.org/wiki/Stable_isotope_composition...

    The isotope effect associated with transamination also makes amino acid nitrogen isotopes a useful tool to study the structure of food webs. Repeated transamination by consumers results in a predictable increase in the abundance of 15 N as amino acids are transferred up food chains. [4]

  5. Side chain - Wikipedia

    en.wikipedia.org/wiki/Side_chain

    Amino acids with similar polarity are usually attracted to each other, while nonpolar and polar side chains usually repel each other. Nonpolar/polar interactions can still play an important part in stabilizing the secondary structure due to the relatively large amount of them occurring throughout the protein. [ 6 ]

  6. Histidine - Wikipedia

    en.wikipedia.org/wiki/Histidine

    Histidine (symbol His or H) [2] is an essential 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 carboxylic acid group (which is in the deprotonated –COO − form under biological conditions), and an imidazole side chain (which is partially protonated), classifying it as a ...

  7. N-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/N-linked_glycosylation

    N-linked glycans are almost always attached to the nitrogen atom of an asparagine (Asn) side chain that is present as a part of Asn–X–Ser/Thr consensus sequence, where X is any amino acid except proline (Pro). [4] In animal cells, the glycan attached to the asparagine is almost inevitably N-acetylglucosamine (GlcNAc) in the β-configuration ...

  8. Glutamine - Wikipedia

    en.wikipedia.org/wiki/Glutamine

    Glutamine (symbol Gln or Q) [3] is an α-amino acid that is used in the biosynthesis of proteins. Its side chain is similar to that of glutamic acid, except the carboxylic acid group is replaced by an amide. It is classified as a charge-neutral, polar amino acid.

  9. Ornithine - Wikipedia

    en.wikipedia.org/wiki/Ornithine

    The amino groups of urea come from the ammonia and aspartate, and the nitrogen in ornithine remains intact. Reaction mechanism:. The side-chain amino group of ornithine (Orn) attacks the carbonyl carbon of carbamoyl phosphate (CP) nucleophilically, left, to form a tetrahedral transition state, middle.

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