NMR Services
1D/2D NMR
Utilized for assessing sample quality, purity, stability, and ligand interactions, offering various screening methods and high-throughput capabilities:
- 1D 1H
- 1D 13C
- 1D 19F
- 1D 31P
- 1D STD/WaterLOGSY/CPMG T2
- 2D TOCSY/NOESY/COSY
- 2D HSQC/HMQC/TROSY/sofast-HMQC
- 2D DOSY
Purification
Ensure protein purity with our automated two-step purification process and diverse purification techniques for challenging proteins.
1D/2D NMR
Utilized for assessing sample quality, purity, stability, and ligand interactions, offering various screening methods and high-throughput capabilities.
Rotational Correlation Time Measurements
Applications include estimating molecular weight, assessing oligomer status, and detecting the presence of antigens in samples for liquid biopsy.
Small Molecule Screening
Detect interactions between small molecules and target protein or RNA, using both ligand-detected and protein/RNA-detected approaches, such as saturation transfer difference (STD), WaterLogsy, 19F, CPMG T2-filtered 19F, and protein-detected chemical shift perturbation studies. Utilizing a cryoprobe, which offers sample volume options ranging from 30-500 µL, along with an automated NMR sampleJet, enables high-throughput screening of ligands, enhancing the efficiency and speed of the detection process.
Protein NMR Resonance Assignments
Correlates chemical shifts to specific atoms, enabling protein structure and dynamics analysis, and ligand binding studies.
Protein Dynamics Studies
NMR can be used to give insights into protein dynamics, entropic changes due to complex formation, and allosteric effects associated with ligand binding.
Protein Interaction Studies
Chemical shift perturbation and/or X-filtered NOESY experiments can be used to detect protein-protein, or protein-ligand interactions.
Nucleic Acid NMR
Probes nucleic acid structure and interactions, facilitating RNA/DNA resonance assignment and compound screening.
NMR Metabolomics Studies
Facilitates metabolomics research, enabling high-throughput identification of metabolites.
Protein NMR structure determination
Elucidating the three-dimensional structure of proteins at atomic resolution, particularly when crystallography is not feasible. Useful for studying small to medium-sized proteins, dynamic regions, protein-ligand interactions, and proteins in environments close to physiological conditions.