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  2. Asparagine - Wikipedia

    en.wikipedia.org/wiki/Asparagine

    Since the asparagine side-chain can form hydrogen bond interactions with the peptide backbone, asparagine residues are often found near the beginning of alpha-helices as asx turns and asx motifs, and in similar turn motifs, or as amide rings, in beta sheets. Its role can be thought as "capping" the hydrogen bond interactions that would ...

  3. Potassium asparaginate - Wikipedia

    en.wikipedia.org/wiki/Potassium_asparaginate

    Potassium asparaginate is a potassium salt of L-asparagine amino acid. [2] [3] [4] [5]Potassium asparaginate can be considered both a salt and a coordination complex. [6] [3] As a salt, potassium asparaginate is formed when the potassium ion (K +) replaces the hydrogen ion (H +) in the carboxyl group of L-asparagine, an amino acid; in this process, the carboxyl group (–COOH) in L-asparagine ...

  4. Asparagine (data page) - Wikipedia

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

    Chemical formula: C 4 H 8 N 2 O 3 Molar mass: 132.118 g·mol −1 Systematic name: (2S)-2-amino-3-carbamoyl-propanoic acid Abbreviations: N, Asn Synonyms: (S)-2-aminosuccinic acid 4-amide {α/2}-aminosuccinamic acid Agedoite Altheine Asparagine acid Asparamide Asparatamine Aspartamic acid Aspartamine Aspartic acid β-amide Aspartic acid amide ...

  5. Hydrophobic collapse - Wikipedia

    en.wikipedia.org/wiki/Hydrophobic_collapse

    A surface exposed alpha helix may have nonpolar residues in an N+3, N+4 position, allowing the alpha-helix to express nonpolar properties on one side when split longitudinally along the axis. Note, in the diagram, the presence of non-polar(gold) amino acids along one side of the helix when viewed through the longitudinal axis, as well as ...

  6. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    Compared to oxygen, sulfur's extra d orbital makes it larger (by 0.4 Å) [29] and softer, allows it to form longer bonds (d C-X and d X-H by 1.3-fold), and gives it a lower pK a (by 5 units). [30] Serine is therefore more dependent than cysteine on optimal orientation of the acid-base triad members to reduce its p K a [ 30 ] in order to achieve ...

  7. Asparagine peptide lyase - Wikipedia

    en.wikipedia.org/wiki/Asparagine_peptide_lyase

    The N-terminal residue of the intein domain must be a serine, threonine or cysteine, and it attacks its preceding peptide bond in order to form an ester or a thioester. The first residue of the second portion of the extein must be a serine, threonine or cysteine as well, and this second nucleophile forms a branched intermediary.

  8. Beta barrel - Wikipedia

    en.wikipedia.org/wiki/Beta_barrel

    The strand order in this barrel (GFP) is: 1 6 5 4 9 8 7 10 11 3 2. The inter-strand hydrogen bonds can be summarised in a table. Each column contains the residues in one strand (strand 1 is repeated in the last column). The arrows indicate the hydrogen bonds that were identified in the figures.

  9. Chemical polarity - Wikipedia

    en.wikipedia.org/wiki/Chemical_polarity

    When comparing a polar and nonpolar molecule with similar molar masses, the polar molecule in general has a higher boiling point, because the dipole–dipole interaction between polar molecules results in stronger intermolecular attractions. One common form of polar interaction is the hydrogen bond, which is also