Substrate interactions between trypanothione reductase and N¹‐glutathionylspermidine disulphide at 0.28‐nm resolution

Keyphrases

• Active Sites 100%
• Trypanothione Reductase 100%
• Disulfide 100%
• Substrate Interaction 100%
• Spermidine 66%
• Hydrogen Bonds (H-bonds) 66%
• Methionine 66%
• Single Crystal 33%
• Leishmania 33%
• Crithidia Fasciculata 33%
• Glutathione 33%
• Trypanosoma 33%
• Tryptophan 33%
• Clinical Application 33%
• Rational Design 33%
• New Inhibitors 33%
• Amino Acid Side Chains 33%
• Tropical Diseases 33%
• Hydrophobic Patch 33%
• Hydrophobic Interaction 33%
• X Ray Diffraction 33%
• Structural Details 33%
• Van Der Waals Interaction 33%
• Extended Conformation 33%
• Bond Length 33%
• Bond Angle 33%
• Diffraction Methods 33%

Biochemistry, Genetics and Molecular Biology

• Enzyme 100%
• Disulfide 100%
• Oxidoreductase 100%
• Reductase 100%
• Active Site 100%
• Substrate Interaction 100%
• Trypanothione 100%
• Methionine 66%
• Amino Acids 33%
• Trypanosoma 33%
• Crithidia fasciculata 33%
• Conformation 33%
• Hydrogen Bond 33%
• Leishmania 33%
• Glutathione 33%
• Tryptophan 33%

Pharmacology, Toxicology and Pharmaceutical Science

• Disulfide 100%
• Trypanothione Reductase 100%
• Spermidine 66%
• Methionine 66%
• Amino Acid 33%
• Leishmania 33%
• Trypanosoma 33%
• Glutathione 33%
• Crithidia fasciculata 33%
• Hydrogen Bond 33%
• Tryptophan 33%
• Bond Length 33%
• Tropical Disease 33%
• Van Der Waals Force 33%