Structural and interactional homology of clinically potential trypsin inhibitors: Molecular modelling of Cucurbitaceae family peptides using the X-ray structure of MCTI-II

Keyphrases

• Molecular Modeling 100%
• Trypsin 100%
• Trypsin Inhibitor 100%
• X-ray Structure 100%
• Cucurbitaceae Family 100%
• High-resolution 16%
• Amino Acids 16%
• Area Studies 16%
• Solution State 16%
• Arginine 16%
• Active Sites 16%
• Amino Acid Residues 16%
• Inhibitory Activity 16%
• Conserved Regions 16%
• Disulfide Bond 16%
• Binding Constant 16%
• Complex Formation 16%
• Energy Profile 16%
• Cucurbitaceae 16%
• Accessible Surface Area 16%
• Biological Needs 16%
• Minor Change 16%
• Homology Modeling 16%
• Inhibitory Peptide 16%
• Active Center 16%
• Binding Behavior 16%
• Bitter Gourd 16%
• Binding Subsites 16%

Biochemistry, Genetics and Molecular Biology

• X Ray 100%
• Molecular Model 100%
• Trypsin Inhibitor 100%
• Cucurbitaceae 100%
• Amino Acids 66%
• Active Site 33%
• Solution and Solubility 33%
• Disulfide Bond 33%
• Homology Modeling 33%
• Binding Affinity 33%
• Accessible Surface Area 33%
• Complex Formation 33%
• Arginine 33%

Immunology and Microbiology

• X Ray 100%
• Molecular Model 100%
• Cucurbitaceae 100%
• Solution and Solubility 50%
• Binding Affinity 50%
• Surface Area 50%
• Complex Formation 50%
• Disulfide Bond 50%