Creative Biostructure to Present at AACR Annual Meeting 2024 Creative Biostructure to Present at AACR Annual Meeting 2024 | April 5-10, 2024 | Booth #2953 Learn More > Close

High-Pressure NMR Service

Inquiry

The combination of high-resolution NMR spectroscopy with pressure perturbation, called variable pressure NMR spectroscopy or high-pressure NMR spectroscopy, is a rapidly developing and promising technique for the future. The importance of this method lies in its ability to systematically detect and analyze the structure and thermodynamic stability of high-energy sub-states in proteins.

13C-edited 1D 1H NMR spectra of L391 Hδ1 recorded at pressures between 20 and 2500 bar.Figure 1. 13C-edited 1D 1H NMR spectra of L391 Hδ1 recorded at pressures between 20 and 2500 bar. (Xu, X.; et al. 2021)

Creative Biostructure has high-end equipment with patented and proprietary design and manufacturing processes, modular design of various accessories for variable temperature, and high-pressure simulations. With high-precision thermostatic probes for more stable data acquisition, our NMR services provide systematic and unique information for a wide range of scientific disciplines.

Service Advantages

  • Large-bore NMR analysis and visualization system
  • Specialized variable temperature and high-pressure probes
  • Ring pressure tracking, pressure accuracy 0.25%
  • Providing information not only on the three-dimensional structure of biomolecules but also on their thermodynamic and kinetic properties, making it an essential tool for understanding the function of biomolecules at atomic resolution
  • Providing the possibility to monitor structural transformations that occur during protein unfolding at atomic resolution and determining the kinetic properties of the process
  • Equipped with modern cryogenic probes to provide unparalleled NMR performance and reliability

Practical Application Examples

  • Transition state measurements in enzyme catalysis.
  • Characterizing protein functional sub-states and protein structures.
  • Understanding the relationship between amino acid sequence, structure, and dynamic properties of the natural conformation of proteins.
  • Understanding the details of protein denaturation and partially folded state conformations and detecting intrinsic protein fluctuations.
  • Quantitative tests to analyze physical parameters such as pore structure, pore size distribution, and movable/bound fluid saturation in unconventional reservoirs.
  • Probing the thermodynamic and kinetic characteristics of proteins interconverting between stable folded conformations.

Creative Biostructure has high-end equipment to provide a full range of high-pressure NMR analysis services to customers in the fields of structural biology and molecular biophysics, helping our customers to obtain unique and in-depth research information. Please feel free to contact us to submit your analytical needs or feedback on our services, and you will receive a satisfactory response soon.

Ordering Process

Ordering Process

Reference

  1. Xu, X.; et al. Volume and compressibility differences between protein conformations revealed by high-pressure NMR. Biophysical Journal. 2021, 120(5): 924-935.

Online Inquiry

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Inquiry