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  2. Serine - Wikipedia

    en.wikipedia.org/wiki/Serine

    Serine (symbol Ser or S) [3] [4] is an α-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 carboxyl group (which is in the deprotonated − COO −

  3. Protein phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphorylation

    Model of a phosphorylated serine residue Serine in an amino acid chain, before and after phosphorylation.. Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group.

  4. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The polar, uncharged amino acids serine (Ser, S), threonine (Thr, T), asparagine (Asn, N) and glutamine (Gln, Q) readily form hydrogen bonds with water and other amino acids. [32] They do not ionize in normal conditions, a prominent exception being the catalytic serine in serine proteases. This is an example of severe perturbation, and is not ...

  5. Complementarity-determining region - Wikipedia

    en.wikipedia.org/wiki/Complementarity...

    Uncharged-polar residues, especially Serine and Tyrosine, are found in CDRs at a high concentration ratio. These residues significantly contribute to the direct hydrogen bonds between the antigen and the antibody. Hydrogen bond interactions will induce the enzymatic activity of an enzyme; therefore, the more hydrogen bonds that are present at ...

  6. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    Serine: S Ser Serine and threonine have a short group ended with a hydroxyl group. Its hydrogen is easy to remove, so serine and threonine often act as hydrogen donors in enzymes. Both are very hydrophilic, so the outer regions of soluble proteins tend to be rich with them. Threonine: T Thr Essential for humans, Thr behaves similarly to serine.

  7. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    The electrostatic states of substrate and active site must be complementary to each other. A polarized negatively charged amino acid side chain will repel uncharged substrate. But if the transition state involves the formation of an ion centre then the side chain will now produce a favourable interaction.

  8. Dying To Be Free - The Huffington Post

    projects.huffingtonpost.com/dying-to-be-free...

    There’s no single explanation for why addiction treatment is mired in a kind of scientific dark age, why addicts are denied the help that modern medicine can offer. Family doctors tend to see addicts as a nuisance or a liability and don’t want them crowding their waiting rooms. In American culture, self-help runs deep.

  9. Serine protease - Wikipedia

    en.wikipedia.org/wiki/Serine_protease

    serine protease reaction mechanism. The main player in the catalytic mechanism in the serine proteases is the catalytic triad. The triad is located in the active site of the enzyme, where catalysis occurs, and is preserved in all superfamilies of serine protease enzymes.