Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints

Lignende værker

• Direct Use of (15)N Relaxation Rates as Experimental Restraints on Molecular Shape and Orientation for Docking of Protein-Protein Complexes
  af: Ryabov, Yaroslav, et al.
  Udgivet: (2010)
• Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation
  af: Clore, G Marius
  Udgivet: (2011)
• Using the Experimentally Determined Components of the Overall Rotational Diffusion Tensor to Restrain Molecular Shape and Size in NMR Structure Determination of Globular Proteins and Protein-Protein Complexes
  af: Ryabov, Yaroslav, et al.
  Udgivet: (2009)
• Nitroxide Labeling of Proteins and the Determination of Paramagnetic Relaxation Derived Distance Restraints for NMR Studies
  af: Sjodt, Megan, et al.
  Udgivet: (2017)
• Coupling between internal dynamics and rotational diffusion in the presence of exchange between discrete molecular conformations
  af: Ryabov, Yaroslav, et al.
  Udgivet: (2012)