What’s in a name? Why these proteins are intrinsically disordered

نویسندگان

  • A. Keith Dunker
  • M. Madan Babu
  • Elisar Barbar
  • Martin Blackledge
  • Sarah E. Bondos
  • Zsuzsanna Dosztányi
  • H. Jane Dyson
  • Julie Forman-Kay
  • Monika Fuxreiter
  • Jörg Gsponer
  • Kyou-Hoon Han
  • David T. Jones
  • Sonia Longhi
  • Steven J. Metallo
  • Ken Nishikawa
  • Ruth Nussinov
  • Zoran Obradovic
  • Rohit V. Pappu
  • Burkhard Rost
  • Philipp Selenko
  • Vinod Subramaniam
  • Joel L. Sussman
  • Peter Tompa
  • Vladimir N Uversky
چکیده

The common view is that functional proteins or protein domains have unique and stable 3D structures characterized by the relatively fixed positions of their atoms and backbone Ramachandran angles that both vary slightly around their equilibrium positions due to low-amplitude thermal fluctuations. In addition there is another class of functional proteins and protein regions that contain smaller or larger highly dynamic fragments, and some proteins are even characterized by a complete or almost complete lack of ordered structure under physiological conditions (at least in vitro) which appears to be a critical aspect of these proteins’ function in vivo. These proteins and protein regions have no single, well-defined equilibrium structure and exist as heterogeneous ensembles of conformers such that no single set of coordinates or backbone Ramachandran angles is sufficient to describe their

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عنوان ژورنال:

دوره 1  شماره 

صفحات  -

تاریخ انتشار 2013