Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Show help for Keywords

Customize results table

Click on the      to add to 'Columns to be displayed' and to the 'Miscellaneous' section below for future use.

    Drag and drop to re-order.


      (max 400 entries)x

      Your basket is currently empty.

      Select item(s) and click on "Add to basket" to create your own collection here
      (400 entries max)

      1 to 1 of 1  Show

      Keywords Results

      Disulfide bond

      Protein which is modified by the formation of a bond between the thiol groups of two peptidyl-cysteine residues. The process of chemical oxidation that forms interchain disulfide bonds can produce stable, covalently linked protein dimers, multimers or complexes, whereas intrachain disulfide bonds can contribute to protein folding and stability. Depending on the protein environment, some disulfide bonds are more labile, forming transient redox-active disulfide bonds that are alternately reduced and oxidized in the course of an enzymatic reaction.

      Category: PTM · UniProtKB (770,934)

      1 to 1 of 1  Show