Nuclear magnetic resonance (NMR) is a key analytical technique for a variety of discovery and analytical applications including small-molecule screening, protein-protein interactions and bio-equivalence. Synbio Technologies offers high quality, customized NMR services including for researchers in life science and pharmaceutical industry. These services include NMR resonance assignments and 3D structures of proteins and complexes. With these services, combined with our advanced molecular biology platforms, Synbio Technologies can handle our customers’ projects starting from gene synthesis all the way to crystallization and structure determination.
- Preparation of stable isotope labeled protein sample
- 1D/2D NMR
- Rotational Correlation Time Measurements
- Small Molecule Screening
- Protein NMR Resonance Assignments
- Protein Dynamics Studies
- Protein Interaction Studies
- Nucleic Acid NMR
Preparation of protein samples with 15N-, 15N13C-, 2H15N13C-, 2H15N13C-ILV-, 19F- specific labeling.
1D/2D NMR can be used to assess sample quality, purity and stability.
NMR screening can also be used to identify interacting ligands and protein partners.
Rotational correlation time is the time it takes a molecule to rotate one radian and it depends on the molecule size.
Application includes: estimation of molecular weight (e.g., oligomerization) and, more recently, to detect presence of antigen in sample in liquid biopsy.
NMR can used to detect small molecule interactions with target proteins using either ligand-detected methods including saturation transfer difference (STD) and WaterLogsy, or protein-detected chemical shift perturbation studies. Ligand screening can then be done with high throughput techniques by using a micro NMR probe (30 uL sample volume) and automated NMR sample changer.
The process describes the correlation of NMR chemical shifts with specific atoms in a protein or other biomolecules. Resonance assignments enable analysis of protein structures and dynamics, as well as studies of ligand binding.
NMR can be used to give insights into protein dynamics, entropic changes due to complex formation, and allosteric effects associated with ligand binding.
Chemical shift perturbation and/or X-filtered NOESY experiments can be used to detect protein-protein or protein-ligand interactions.
NMR can be used to probe nucleic acid structure and interactions.
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