Now showing items 1-3 of 3

    • 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
    • WEBnm@ v2.0: Web server and services for comparing protein flexibility 

      Tiwari, Sandhya Premnath; Fuglebakk, Edvin; Hollup, Siv Midtun; Skjærven, Lars; Cragnolini, Tristan; Grindhaug, Svenn Helge; Tekle, Kidane M; Reuter, Nathalie (BioMed Central, 2014-12-30)
      Background: Normal mode analysis (NMA) using elastic network models is a reliable and cost-effective computational method to characterise protein flexibility and by extension, their dynamics. Further insight into the ...
      Journal article