Heat Capacity Changes for Transition-State Analogue Binding and Catalysis with Human 5′-Methylthioadenosine Phosphorylase

Medicine & Life Sciences

• 5'-methylthioadenosine phosphorylase 100%
• Catalysis 67%
• 4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin A 60%
• Hot Temperature 43%
• Tubercidin 29%
• 5'-methylthioadenosine 28%
• Temperature 23%
• Apoenzymes 12%
• Calorimetry 11%
• S-Adenosylmethionine 10%
• Entropy 9%
• Polyamines 9%
• Protein Stability 9%
• Molecular Dynamics Simulation 9%
• Hydrophobic and Hydrophilic Interactions 8%
• Physiological Phenomena 8%
• Spectrum Analysis 7%
• Catalytic Domain 7%
• Kinetics 5%
• Ligands 5%
• Proteins 2%

Chemical Compounds

• Heat Capacity 57%
• Catalysis 36%
• Transition State 23%
• Isothermal Titration Calorimetry 15%
• Polyamine 15%
• Dissociation Constant 13%
• Hydrophobicity 12%
• Protein 11%
• Entropy 11%
• Enthalpy 11%
• Molecular Dynamics 10%
• Thermal Stability 9%
• Spectroscopy 9%
• Simulation 8%
• Chemistry 8%
• Crystal Structure 7%
• Ligand 6%