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Virtual Lead Selectivity Test
The Quantum Lead Selectivity Test explores potential selectivity of a drug candidate, adverse activity and additional unexpected activity by screening it in silico against thousands of proteins.
For each protein, the IC50 value is calculated, thus, the activity of the drug candidate is predicted. We apply our proprietary developed computational technology QUANTUM, which shows outstanding accuracy in forecasting binding affinities. The hit rate of the QUANTUM performance is about 50%, it means that a half of found in silico strong inhibitors would be confirmed in in-vitro testing!!!
This service provides a web interface to select a set of proteins for screening purposes. The default profile contains of about 1000 proteins. Click to access the Lead Selectivity Web Interface.
The outstanding accuracy of Quantum calcaulations reduce greatly need to use in-vitro binding assay, inhibition assay for activity testing research.
With the demand to “fail fast, fail cheap”, our Lead selectivity testcan help you to make decisions regarding the further drug development pathway and strategy —which entities to pursue or which to withdraw.
Note that you can also purchase the Lead Selectivity Module However; this module requires significant computational recourses. For detail information, please contact us.
Click to download Lead Selectivity Module overview brochure
With Quantum Lead Selectivity technology platform you can make an in-silico compound profiling study to explore how your compound will interact with many macromolecule structures, e.g. including
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Title: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS |
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Functional Class: Hydrolase Primary citation: Funahashi, J.,Takano, K.,Yamagata, Y.,Yutani, K. Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. Biochemistry v39 pp.14448-14456, 2000 |
Abstract Title: Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions.
Keywords: Lysozyme, D1gf9a_, Support, (a+b), Humans, Research, Thermodynamics, Enzyme, Methionine, Membrane, (homo, Site-directed, Hydrolase, Muramidase, Catabolism, Orthogonal, Conformation, Bundle, Cell, Wall, Sapiens), Differential, Valine, C-type, Alpha, 1gf9a0, Extracellular, Sapiens, Acids, Leucine, Calorimetry, Mutagenesis, Lysozyme, Substitution, Proteins, Beta, Alanine, Non-u.s., Isoleucine, Scanning, Acid, Glycine, Region, Sodium, Proteins, (1gf9:a), Phenylalanine, Stability, Lysozyme-like, Homo, Human, Activity, Mainly, Protein, Crystallography, Gov't, Lysozyme, X-ray, Amino, Binding assay, Inhibition assay, Activity testing research,
