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

Lignende værker

• 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
  af: Chen, Shuai, et al.
  Udgivet: (2008)
• Residues on the Dimer Interface of SARS Coronavirus 3C-like Protease: Dimer Stability Characterization and Enzyme Catalytic Activity Analysis
  af: Chen, Shuai, et al.
  Udgivet: (2008)
• pH-dependent Conformational Flexibility of the SARS-CoV Main Proteinase (M(pro)) Dimer: Molecular Dynamics Simulations and Multiple X-ray Structure Analyses
  af: Tan, Jinzhi, et al.
  Udgivet: (2005)
• In vitro biochemical and thermodynamic characterization of nucleocapsid protein of SARS
  af: Luo, Haibin, et al.
  Udgivet: (2004)
• Techniques used for the discovery of therapeutic compounds: The case of SARS
  af: Chen, Shuai, et al.
  Udgivet: (2006)