Now showing items 1-4 of 4

    • Binding Leverage as a Molecular Basis for Allosteric Regulation 

      Mitternacht, Simon; Berezovsky, Igor N. (Public Library of Science, 2011-09-15)
      Allosteric regulation involves conformational transitions or fluctuations between a few closely related states, caused by the binding of effector molecules. We introduce a quantity called binding leverage that measures ...
      Peer reviewedJournal article
    • Coherent Conformational Degrees of Freedom as a Structural Basis for Allosteric Communication 

      Mitternacht, Simon; Berezovsky, Igor N. (Public Library of Science, 2011-12-08)
      Conformational changes in allosteric regulation can to a large extent be described as motion along one or a few coherent degrees of freedom. The states involved are inherent to the protein, in the sense that they are ...
      Peer reviewedJournal article
    • A geometry-based generic predictor for catalytic and allosteric sites 

      Mitternacht, Simon; Berezovsky, Igor N. (Oxford University Press, 2011)
      An important aspect of understanding protein allostery, and of artificial effector design, is the characterization and prediction of substrate- and effector-binding sites. To find binding sites in allosteric enzymes, many ...
      Journal articlePeer reviewed
    • The Methylococcus capsulatus (Bath) Secreted Protein, MopE*, Binds Both Reduced and Oxidized Copper 

      Ve, Thomas; Mathisen, Karina; Helland, Ronny; Karlsen, Odd André; Fjellbirkeland, Anne; Røhr, Åsmund K.; Andersson, K. Kristoffer; Pedersen, Rolf Birger; Lillehaug, Johan; Jensen, Harald B. (Public Library of Science (PLoS), 2012-08-20)
      Under copper limiting growth conditions the methanotrophic bacterium Methylococcus capsulatus (Bath) secrets essentially only one protein, MopE*, to the medium. MopE* is a copper-binding protein whose structure has been ...
      Journal articlePeer reviewed