Mast cell tryptases: examination of unusual characteristics by multiple sequence alignment and molecular modeling

Keyphrases

• Molecular Modeling 100%
• Multiple Sequence Alignment 100%
• Mast Cell Tryptase 100%
• Tryptase 100%
• Trypsin 37%
• Active Sites 25%
• Heparin Binding 25%
• Serine Proteinase 25%
• 3D Structure 12%
• Site-directed mutagenesis 12%
• Sequence Identity 12%
• Protein Substrate 12%
• Unique Sequences 12%
• Glycosylation Site 12%
• Heparin 12%
• Rational Basis 12%
• Sequence Features 12%
• Synthetic Substrate 12%
• Hydrophobic Patch 12%
• Mast Cells 12%
• Natural Inhibitors 12%
• Large Insertion 12%
• Granules 12%
• Structural Explanation 12%
• Proline-rich Region 12%
• Trypsin Inhibitor 12%
• Trypsin-like 12%
• Bovine Trypsin 12%

Biochemistry, Genetics and Molecular Biology

• Molecular Model 100%
• Sequence Alignment 100%
• Tryptase 100%
• Heparin 33%
• Active Site 22%
• Serine Protease 22%
• Crystal Structure 11%
• Site-Directed Mutagenesis 11%
• Glycosylation 11%
• Mast Cell 11%
• Trypsin Inhibitor 11%
• Proline 11%
• Arginine 11%

Immunology and Microbiology

• Molecular Model 100%
• Mast Cell 100%
• Sequence Alignment 100%
• Site Directed Mutagenesis 50%
• Glycosylation 50%
• Crystal Structure 50%