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  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Amino acids with the structure NH + 3 −CXY−CXY−CO − 2, such as β-alanine, a component of carnosine and a few other peptides, are β-amino acids. Ones with the structure NH + 3 −CXY−CXY−CXY−CO − 2 are γ-amino acids, and so on, where X and Y are two substituents (one of which is normally H). [7]

  3. Isobutanol - Wikipedia

    en.wikipedia.org/wiki/Isobutanol

    Isobutanol (IUPAC nomenclature: 2-methylpropan-1-ol) is an organic compound with the formula (CH 3) 2 CHCH 2 OH (sometimes represented as i-BuOH). This colorless, flammable liquid with a characteristic smell is mainly used as a solvent either directly or as its esters.

  4. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the ...

  5. Butanol - Wikipedia

    en.wikipedia.org/wiki/Butanol

    Butanol (also called butyl alcohol) is a four-carbon alcohol with a formula of C 4 H 9 O H, which occurs in five isomeric structures (four structural isomers), from a straight-chain primary alcohol to a branched-chain tertiary alcohol; [1] all are a butyl or isobutyl group linked to a hydroxyl group (sometimes represented as BuOH, sec-BuOH, i-BuOH, and t-BuOH).

  6. Acid–base homeostasis - Wikipedia

    en.wikipedia.org/wiki/Acid–base_homeostasis

    Acid–base homeostasis is the homeostatic regulation of the pH of the body's extracellular fluid (ECF). [1] The proper balance between the acids and bases (i.e. the pH) in the ECF is crucial for the normal physiology of the body—and for cellular metabolism. [1]

  7. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    One of the purposes of this field of study is to determine which proteins are glycosylated and where in the amino acid sequence the glycosylation occurs. [4] Historically, mass spectrometry has been used to identify the structure of glycoproteins and characterize the carbohydrate chains attached. [4] [10]

  8. Phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Phosphorylation

    Serine in an amino acid chain, before and after phosphorylation. In biochemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion. [1] This process and its inverse, dephosphorylation, are common in biology. [2] Protein phosphorylation often activates (or deactivates) many enzymes. [3] [4]

  9. Glucogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Glucogenic_amino_acid

    Glucogenic amino acids can be converted into intermediates that feed the gluconeogenesis metabolic pathway, which produces glucose. When necessary, these amino acids can be used to generate glucose. As previously stated, because they can be transformed into glucose via a variety of metabolic pathways, the majority of amino acids (apart from ...