Protein NMR spectroscopy services

1. Protein NMR spectroscopy services

2. NMR spectroscopy is a key analytical technique for the structure elucidation of a wide range of materials from small molecules to compounds. The technique provides detailed molecular information that allows researchers to have an in-depth understanding of composition, chemical structure, morphology, and dynamics. NMR is particularly useful in the analysis of pharmaceuticals, screening weak-binding compounds and developing into drug-like inhibitors for drug discovery. Supported by our NMR platform, Creative Biostructure offers high-quality customized NMR spectroscopy services ranging from the production of labeled-proteins to acquisition and analysis of high-field NMR data for researchers in the science and pharmaceutical industry.

4. Advantages of Protein NMR Spectroscopy • For proteins that are hard to obtain single crystals because of their high flexibility, NMR spectroscopy is an alternative approach to obtain high-resolution structures. • It can measure the three-dimensional structure of biological macromolecules with atomic resolution under membrane mimetic states or almost physiological environments, especially structural analysis of low-molecular-weight proteins. • It is an appropriate strategy for obtaining information on intermolecular interactions and biomolecular dynamics and for investigating the structure of folded intermediates and the residual structure of unfolded proteins. • Low-transient and low-affinity complexes and small protein-ligand interactions can be studied by NMR spectroscopy.

5. The Workflow of Our Protein NMR Spectroscopy Services

6. Other NMR Spectroscopy Services at Creative Biostructure • Chemical Composition Determination • Molecular Characterization • Reaction Kinetics Examination • Dynamics and Disorder Analysis • NMR Mapping of Protein Interactions in Living Cells • Mapping Structure of Biological Drugs • NMR Analysis for Biopharmaceutical Development

7. Combining NMR and Mass Spectrometry for Metabolomics • Stable Isotope Labeling for Proteins • Stable Isotope Labeling for Nucleic Acids • 4D NMR Services • Solid-state NMR Services • LF-NMR/TD-NMR Services

8. NMR Sample Preparation Guideline • The protein samples for structural analysis can be obtained from customers or produced by us. For larger proteins, we support the production of isotope-labeled NMR samples. • Labeling with isotopes: Protein NMR spectroscopy requires isotope enrichment, such as 15N, 13C, 31P, 19F in common. Samples with other isotopes are also acceptable. • Size: The molecular weight of the biomacromolecule of an NMR sample is typically less than 50 KDa for high-resolution structure elucidation. Larger proteins or complexes can be studied to identify ligand/drug-binding sites or to characterize the physical state.

9. Amount: For solution NMR, a sample typically contains 1-10 mg/ml or 0.3 mM purified protein in a suitable buffer; for solid-state NMR, we require a larger amount of samples, please talk to our specialist for more information. • Stability: For most in-depth studies by NMR, the protein needs to be stable for several days at room temperature for data acquisition.

10. Reference • Xiao S, et al. Tom1 modulates binding of tollip to phosphatidylinositol 3-phosphate via a coupled folding and binding mechanism. Structure. 2015, 23(10): 1910-1920.

11. Excerpt from: https://www.creative-biostructure.com/nmr-services_28.htm