• Question: Hi Toby, I've seen you mentioned that you are currently interested in Chaperone, which assists the non-covalent folding of proteins. Hence, I am wondering that, as a tertiary (or even quaternary protein), how is Chaperone folded itself in the first place? Or, alternatively, do all folding processes require assistant? Thanks!!

    Asked by amandazzh to Toby on 20 Jun 2014.
    • Photo: Tobias Warnecke

      Tobias Warnecke answered on 20 Jun 2014:

      Hi amandazzh,

      that’s a fantastic question!

      I guess the first important bit of information is that many proteins can fold pretty well by themselves. In E. coli, for example, where protein folding is best understood, about 70% of proteins don’t seem to require any/much help in finding their right 3D structure – which is pretty remarkable. Other proteins take a bit longer to fold without a chaperone but get there eventually.
      Some chaperones belong to the group that folds pretty well by itself, and these chaperones can then help other chaperones to fold.

      Finally, when cells divide and a new cell is created, that new cell will inherit some of the chaperones from the mother cell so it doesn’t have to start from scratch.

      Is that the explanation you were looking for?

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