Distance-constraint approach to protein folding. II. Prediction of three-dimensional structure of bovine pancreatic trypsin inhibitor

Medicine & Life Sciences

• Aprotinin 89%
• Protein Folding 80%
• Amino Acids 48%
• Sulfur 40%
• Hydrophobic and Hydrophilic Interactions 37%
• Aromatic Amino Acids 24%
• Disulfides 18%
• Catalytic Domain 15%
• Proteins 6%

Engineering & Materials Science

• Protein folding 100%
• Conformations 86%
• Amino acids 67%
• Sulfur 21%
• Carboxylic acids 17%
• Hydrophilicity 16%
• Hydrophobicity 14%
• Atoms 11%
• Proteins 10%
• Geometry 6%

Chemical Compounds

• Trypsin Inhibitor 82%
• Protein Folding 74%
• Amino-Acid Residue 61%
• Aromatic Amino Acid 15%
• Sulfur Atom 13%
• Hydrophilicity 12%
• Hydrophobicity 11%
• Disulfide 11%
• Protein 5%