Pages that link to "Q72858679"
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The following pages link to Locating the catalytic water molecule in serine proteases (Q72858679):
Displaying 13 items.
- Trypsin revisited: crystallography AT (SUB) atomic resolution and quantum chemistry revealing details of catalysis (Q27641895) (← links)
- Structure of a serine protease poised to resynthesize a peptide bond (Q27643959) (← links)
- A mechanistic view of enzyme inhibition and peptide hydrolysis in the active site of the SARS-CoV 3C-like peptidase (Q27646489) (← links)
- Structure of a specific acyl-enzyme complex formed between beta-casomorphin-7 and porcine pancreatic elastase (Q27739099) (← links)
- Protein sectors: evolutionary units of three-dimensional structure (Q28256199) (← links)
- Desiccation tolerance of prokaryotes (Q28776135) (← links)
- Atlas of coronavirus replicase structure. (Q30357066) (← links)
- Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates (Q34598232) (← links)
- Bi-factor analysis based on noise-reduction (BIFANR): a new algorithm for detecting coevolving amino acid sites in proteins (Q35053259) (← links)
- Cluster analysis of consensus water sites in thrombin and trypsin shows conservation between serine proteases and contributions to ligand specificity (Q36280688) (← links)
- Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects (Q38327973) (← links)
- Molecular dynamics simulations of the acyl-enzyme and the tetrahedral intermediate in the deacylation step of serine proteases (Q43956367) (← links)
- Mechanistic insights from molecular dynamic simulation of Rv0045c esterase in Mycobacterium tuberculosis (Q50851120) (← links)