Structure-based thermodynamic design of peptide ligands: Application to peptide inhibitors of the aspartic protease endothiapepsin

Medicine & Life Sciences

• Endothia aspartic proteinase 100%
• pepstatin 69%
• Thermodynamics 55%
• Protease Inhibitors 47%
• Ligands 32%
• Peptides 29%
• Molecular Structure 11%
• Mutation 10%
• Phenylalanine 10%
• Alanine 9%
• Glutamic Acid 8%
• Amino Acids 6%

Chemical Compounds

• Pepstatin 68%
• Thermodynamics 28%
• Gibbs Free Energy 20%
• Ligand 19%
• Mutation 15%
• Aspartic Proteinase Inhibitor 15%
• Application 14%
• Phenylalanine 9%
• Alanine 8%
• Kd 6%
• Length 5%
• Modification 5%
• Acid 3%