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  2. Peptide bond - Wikipedia

    en.wikipedia.org/wiki/Peptide_bond

    Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.

  3. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    In this modification, an asparagine or aspartate side chain attacks the following peptide bond, forming a symmetrical succinimide intermediate. Hydrolysis of the intermediate produces either aspartate or the β-amino acid, iso(Asp). For asparagine, either product results in the loss of the amide group, hence "deamidation". hydroxylation

  4. Peptide - Wikipedia

    en.wikipedia.org/wiki/Peptide

    Drosomycin, an example of a peptide. Peptides are short chains of amino acids linked by peptide bonds. [1] [2] A polypeptide is a longer, continuous, unbranched peptide chain. [3] Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. [4]

  5. Biochemistry - Wikipedia

    en.wikipedia.org/wiki/Biochemistry

    In this dehydration synthesis, a water molecule is removed and the peptide bond connects the nitrogen of one amino acid's amino group to the carbon of the other's carboxylic acid group. The resulting molecule is called a dipeptide , and short stretches of amino acids (usually, fewer than thirty) are called peptides or polypeptides .

  6. Chemical specificity - Wikipedia

    en.wikipedia.org/wiki/Chemical_specificity

    A reaction that illustrates an enzyme cleaving a specific bond of the reactant in order to create two products Bond specificity, unlike group specificity, recognizes particular chemical bond types. This differs from group specificity, as it is not reliant on the presence of particular functional groups in order to catalyze a particular reaction ...

  7. Biomolecular structure - Wikipedia

    en.wikipedia.org/wiki/Biomolecular_structure

    Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits.

  8. Translation (biology) - Wikipedia

    en.wikipedia.org/wiki/Translation_(biology)

    Aminoacyl tRNA synthetases catalyze the bonding between specific tRNAs and the amino acids that their anticodon sequences call for. The product of this reaction is an aminoacyl-tRNA. The amino acid is joined by its carboxyl group to the 3' OH of the tRNA by an ester bond. When the tRNA has an amino acid linked to it, the tRNA is termed "charged".

  9. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    Amino acid side chains and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure.