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  2. Peptide synthesis - Wikipedia

    en.wikipedia.org/wiki/Peptide_synthesis

    In organic chemistry, peptide synthesis is the production of peptides, compounds where multiple amino acids are linked via amide bonds, also known as peptide bonds. Peptides are chemically synthesized by the condensation reaction of the carboxyl group of one amino acid to the amino group of another.

  3. Protein biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Protein_biosynthesis

    Once synthesis of the polypeptide chain is complete, the polypeptide chain folds to adopt a specific structure which enables the protein to carry out its functions. The basic form of protein structure is known as the primary structure, which is simply the polypeptide chain i.e. a sequence of covalently bonded amino acids. The primary structure ...

  4. Peptide library - Wikipedia

    en.wikipedia.org/wiki/Peptide_library

    Large random peptide libraries are often used for the synthesis of certain peptide molecules, such as ultra-large chemical libraries for the discovery of high-affinity peptide binders. [4] Any increase in the library size severely affects parameters, such as the synthesis scale, the number of library members, the sequence deconvolution and ...

  5. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    The image above contains clickable links This diagram (which is interactive) of protein structure uses PCNA as an example. ( PDB : 1AXC ) Protein structure is the three-dimensional arrangement of atoms in an amino acid -chain molecule .

  6. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Intramolecular transesterification, resulting in a branched polypeptide. In inteins, the new ester bond is broken by an intramolecular attack by the soon-to-be C-terminal asparagine. Intermolecular transesterification can transfer a whole segment from one polypeptide to another, as is seen in the Hedgehog protein autoprocessing.

  7. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    The image above contains clickable links This diagram (which is interactive) of protein structure uses PCNA as an example. (The tertiary structure of a protein consists of the way a polypeptide is formed of a complex molecular shape. This is caused by R-group interactions such as ionic and hydrogen bonds, disulphide bridges, and hydrophobic ...

  8. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Polypeptide chains fold in a particular manner depending on the solution they are in. The fact that all amino acids contain R groups with different properties is the main reason proteins fold. In a hydrophilic environment such as cytosol , the hydrophobic amino acids will concentrate at the core of the protein, while the hydrophilic amino acids ...

  9. Biomolecular structure - Wikipedia

    en.wikipedia.org/wiki/Biomolecular_structure

    The primary structure of a biopolymer is the exact specification of its atomic composition and the chemical bonds connecting those atoms (including stereochemistry).For a typical unbranched, un-crosslinked biopolymer (such as a molecule of a typical intracellular protein, or of DNA or RNA), the primary structure is equivalent to specifying the sequence of its monomeric subunits, such as amino ...