Thermodynamic basis of resistance to HIV-1 protease inhibition: Calorimetric analysis of the V82F/I84V active site resistant mutant

Medicine & Life Sciences

• Human immunodeficiency virus 1 p16 protease 100%
• Thermodynamics 81%
• Entropy 80%
• Protease Inhibitors 69%
• Catalytic Domain 60%
• Ritonavir 56%
• Binding Sites 51%
• Peptide Hydrolases 37%
• Burial 33%
• Nelfinavir 33%
• Saquinavir 32%
• Indinavir 31%
• Mutation 25%
• HIV Infections 19%
• HIV-1 19%
• Therapeutics 3%

Chemical Compounds

• Protease Inhibitor 59%
• Ritonavir 51%
• Kd 50%
• Resistance 42%
• Thermodynamics 41%
• Entropy 41%
• Enthalpy 39%
• Binding Site 35%
• Mutation 28%
• Nelfinavir 28%
• Saquinavir 27%
• Indinavir 27%
• Hydrophobic Surface 18%
• Strain 11%
• Force 11%
• Energy 7%