We provide comprehensive nuclear magnetic resonance (NMR) spectroscopy services for the characterization of small molecules, natural products, proteins, nucleic acids and other biomolecular systems. Services range from routine spectral acquisition to advanced structural, biophysical and drug-discovery applications.
NMR Services
Includes 1D, 2D, 3D, and higher-dimensional experiments.
Experiments for structural and functional characterization.
Includes organic small molecules, natural products, peptides, proteins, DNA, RNA, and other macromolecules.
Includes assessment of sample quality, purity, stability, solubility, aggregation, conformational state, and protein folding.
Includes ligand-binding assays, protein–ligand interactions, binding-site characterization, and competition experiments.
For rapid and sensitive identification of small-molecule fragments that interact with a target protein. Services can include assay development and optimization, screening of fluorinated fragment libraries, identification of primary hits, competition or displacement experiments, and follow-up validation of fragment binding.
Includes primary fragment screening, hit confirmation, binding characterization, structure–activity relationship support, and prioritization of fragments for downstream medicinal chemistry and lead development.
Using NMR-based approaches to evaluate compound binding, compare analogs, characterize molecular interactions, and support optimization of lead compounds.
To investigate molecular interactions, conformational exchange, reaction kinetics, and changes in molecular structure or dynamics.
Of small molecules and biomolecules using appropriate multidimensional NMR approaches.
Including optimization of experimental conditions, sample concentrations, buffer conditions, acquisition parameters, and controls for biochemical and drug-discovery applications.
Includes assistance with selecting appropriate NMR experiments and setting up data acquisition.
Includes spectral processing, peak assignment, comparison of spectra, identification of binding-induced changes, and interpretation of NMR results.
In NMR spectroscopy, including sample preparation, instrument operation, experiment setup, data acquisition, processing, analysis, and interpretation.
Sample Preparation
- Provide recommendations on isotope labeling strategies for structural and dynamic studies
- Protein buffer optimization