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
  • Exploring the evolution of protein function in Archaea 

    Goncearenco, Alexander; Berezovsky, Igor N. (BioMed Central, 2012-05-30)
    Background: Despite recent progress in studies of the evolution of protein function, the questions what were the first functional protein domains and what were their basic building blocks remain unresolved. Previously, we ...
    Journal 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