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  2. Nisin - Wikipedia

    en.wikipedia.org/wiki/Nisin

    Nisin is a polycyclic antibacterial peptide produced by the bacterium Lactococcus lactis that is used as a food preservative.It has 34 amino acid residues, including the uncommon amino acids lanthionine (Lan), methyllanthionine (MeLan), didehydroalanine (Dha), and didehydroaminobutyric acid (Dhb).

  3. Peptide amphiphile - Wikipedia

    en.wikipedia.org/wiki/Peptide_amphiphile

    Peptide amphiphiles were developed in the 1990s. They were first described by the group of Matthew Tirrell in 1995. [5] [6] These first reported PA molecules were composed of two domains: one of lipophilic character and another of hydrophilic properties, which allowed self-assembly into sphere-like supramolecular structures as a result of the association of the lipophilic domains away from the ...

  4. Peptide synthesis - Wikipedia

    en.wikipedia.org/wiki/Peptide_synthesis

    The established method for the production of synthetic peptides in the lab is known as solid phase peptide synthesis (SPPS). [2] Pioneered by Robert Bruce Merrifield, [4] [5] SPPS allows the rapid assembly of a peptide chain through successive reactions of amino acid derivatives on a macroscopically insoluble solvent-swollen beaded resin support.

  5. 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]

  6. List of recombinant proteins - Wikipedia

    en.wikipedia.org/wiki/List_of_recombinant_proteins

    A much larger number of recombinant proteins is used in the research laboratory. These include both commercially available proteins (for example most of the enzymes used in the molecular biology laboratory), and those that are generated in the course specific research projects.

  7. Ribosomally synthesized and post-translationally modified ...

    en.wikipedia.org/wiki/Ribosomally_synthesized...

    This peptide consists of a core peptide segment which is typically preceded (and occasionally followed) by a leader peptide segment and is typically ~20-110 residues long. The leader peptide is usually important for enabling enzymatic processing of the precursor peptide via aiding in recognition of the core peptide by biosynthetic enzymes and ...

  8. Oligopeptide - Wikipedia

    en.wikipedia.org/wiki/Oligopeptide

    An oligopeptide (oligo-, "a few"), is a peptide consisting of two to twenty amino acids, including dipeptides, tripeptides, tetrapeptides, and other polypeptides. Some of the major classes of naturally occurring oligopeptides include aeruginosins , cyanopeptolins , microcystins , microviridins , microginins , anabaenopeptins , and cyclamides .

  9. Nonribosomal peptide - Wikipedia

    en.wikipedia.org/wiki/Nonribosomal_peptide

    Nonribosomal peptides are also found in higher organisms, such as nudibranchs, but are thought to be made by bacteria inside these organisms. [1] While there exist a wide range of peptides that are not synthesized by ribosomes, the term nonribosomal peptide typically refers to a very specific set of these as discussed in this article.