Mutation of Gly-11 on the Dimer Interface Results in the Complete Crystallographic Dimer Dissociation of Severe Acute Respiratory Syndrome Coronavirus 3C-like Protease: CRYSTAL STRUCTURE WITH MOLECULAR DYNAMICS SIMULATIONS

Παρόμοια τεκμήρια

• Residues on the Dimer Interface of SARS Coronavirus 3C-like Protease: Dimer Stability Characterization and Enzyme Catalytic Activity Analysis
  ανά: Chen, Shuai, κ.ά.
  Έκδοση: (2008)
• Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure()
  ανά: Hu, Tiancen, κ.ά.
  Έκδοση: (2009)
• Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase N Terminus Is Indispensable for Proteolytic Activity but Not for Enzyme Dimerization: BIOCHEMICAL AND THERMODYNAMIC INVESTIGATION IN CONJUNCTION WITH MOLECULAR DYNAMICS SIMULATIONS
  ανά: Chen, Shuai, κ.ά.
  Έκδοση: (2005)
• Structure of the SARS coronavirus main proteinase as an active C(2) crystallographic dimer
  ανά: Xu, Ting, κ.ά.
  Έκδοση: (2005)
• The Catalytic Intermediate Stabilized by a “Down” Active Site Loop for Diaminopimelate Decarboxylase from Helicobacter pylori: ENZYMATIC CHARACTERIZATION WITH CRYSTAL STRUCTURE ANALYSIS
  ανά: Hu, Tiancen, κ.ά.
  Έκδοση: (2008)