Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations

Lignende værker

• Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations
  af: Huan, Xuelu, et al.
  Udgivet: (2013)
• Structural, Stability, Dynamic and Binding Properties of the ALS-Causing T46I Mutant of the hVAPB MSP Domain as Revealed by NMR and MD Simulations
  af: Lua, Shixiong, et al.
  Udgivet: (2011)
• NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics
  af: Gupta, Garvita, et al.
  Udgivet: (2015)
• Crystal Structure and NMR Binding Reveal That Two Small Molecule Antagonists Target the High Affinity Ephrin-binding Channel of the EphA4 Receptor
  af: Qin, Haina, et al.
  Udgivet: (2008)
• Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes
  af: Qin, Haina, et al.
  Udgivet: (2014)