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  2. Disulfide - Wikipedia

    en.wikipedia.org/wiki/Disulfide

    That is, the disulfide bond destabilizes the unfolded form of the protein by lowering its entropy. The disulfide bond may form the nucleus of a hydrophobic core of the folded protein, i.e., local hydrophobic residues may condense around the disulfide bond and onto each other through hydrophobic interactions.

  3. Post-translational modification - Wikipedia

    en.wikipedia.org/wiki/Post-translational...

    The formation of disulfide bonds from cysteine residues may also be referred to as a post-translational modification. [3] For instance, the peptide hormone insulin is cut twice after disulfide bonds are formed, and a propeptide is removed from the middle of the chain; the resulting protein consists of two polypeptide chains connected by ...

  4. Sulfide - Wikipedia

    en.wikipedia.org/wiki/Sulfide

    Carbon disulfide is a precursor to organosulfur compounds. −111.6: 46: 75-15-0: PbS: Lead sulfide is used in infra-red sensors. 1114: 1314-87-0: MoS 2: Molybdenum disulfide, the mineral molybdenite, is used as a catalyst to remove sulfur from fossil fuels; also as lubricant for high-temperature and high-pressure applications. 1317-33-5: Cl ...

  5. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    However, proteins can become cross-linked, most commonly by disulfide bonds, and the primary structure also requires specifying the cross-linking atoms, e.g., specifying the cysteines involved in the protein's disulfide bonds. Other crosslinks include desmosine.

  6. Dithiothreitol - Wikipedia

    en.wikipedia.org/wiki/Dithiothreitol

    DTT is a reducing agent; once oxidized, it forms a stable six-membered ring with an internal disulfide bond.It has a redox potential of −0.33 V at pH 7. [1] The reduction of a typical disulfide bond proceeds by two sequential thiol-disulfide exchange reactions and is illustrated below.

  7. Cysteine - Wikipedia

    en.wikipedia.org/wiki/Cysteine

    Inside the cell, disulfide bridges between cysteine residues within a polypeptide support the protein's tertiary structure. Insulin is an example of a protein with cystine crosslinking, wherein two separate peptide chains are connected by a pair of disulfide bonds.

  8. AOL Mail for Verizon Customers - AOL Help

    help.aol.com/products/aol-mail-verizon

    AOL Mail welcomes Verizon customers to our safe and delightful email experience!

  9. Lipoic acid - Wikipedia

    en.wikipedia.org/wiki/Lipoic_acid

    Lipoic acid contains two sulfur atoms connected by a disulfide bond in the 1,2-dithiolane ring. It also carries a carboxylic acid group. It is considered to be oxidized relative to its acyclic relative dihydrolipoic acid, in which each sulfur exists as a thiol. [3] It is a yellow solid.