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The University of Kentucky PharmNMR Center located in Room B003 of the Lee T. Todd Jr. Building which houses the UK College of Pharmacy. We have three solution NMR spectrometers, including an MR400, VNMRS500, and Bruker 600 AV4 NEO. These are available via our cost-recharge center and may be utilized by any university or industry researcher. 

1D, 2D, and 3D NMR data acquisition, processing, and data analysis of small molecules and biomolecules (3D structure determination of peptides and proteins, protein-protein interactions, and protein-ligand interactions) can be carried over upon request with an appropriate per hour recharge fee. Carbon detected experiments can be done for those who are interested to investigate their intrinsically disordered proteins (IDP) structures and dynamics studies.

All College of Pharmacy NMR users wanting to use TopSpin/protein dynamics, VNMR, nmrPipe and SPARKY software for themselves – an off-line data processing station is available in the basement in front of the PharmNMR room.

Instrument Sensitivity for Different Nuclei

Instrument

1H

13C 15N
MR400 400 180 21
VNMRS500 2235 140 35
Brucker 600 AV4 NEO 8300 1200 105

 

  • Most commonly used experiments on MR400 to characterize small molecules: Homonuclear (1H) and heteronuclear 1D (1H, 13C, 31P, 15N, and 19F) such as 1H, DOSY, 13C-DEPT, APT, 31P, 15N, 19F; and 2D NMR experiments such as COSY, DQF-COSY, NOESY, ROESY, TOCSY, HSQC, HMBC, INADEQUATE, and diffusion ordered spectroscopy.
  • Sensitivity specifications: The probe sensitivity for 1H is 400:1; 13C is 180:1; 15N is 21:1 and 19F is 550:1.
  • NMR software used: VNMR 4.2
  • Most commonly used experiments on VNMRS500 to characterize small molecules and smaller size biomolecules: Homonuclear (1H) and heteronuclear (1H, 13C, or 15N) 1D (1H, 13C-DEPT, APT, 15N) and 2D NMR experiments: COSY, DQF-COSY, NOESY, ROESY, TOCSY, 1H-13C HSQC, 1H-15N HSQC, 1H-13C HMBC, INADEQUATE, and diffusion ordered spectroscopy (DOSY).
  • Sensitivity specifications: The probe sensitivity for 1H is 2235:1; 13C is 140:1; and 15N is 35:1.
  • NMR software used: VNMR 4.2
  • Unprecedented signal-to-noise (S/N) or sensitivity gain up to 4x and lower detection limits over a room-temperature probe
  • Up to ~ 20x reduction in data collection time for high-resolution liquid applications 
  • 5-mm 1H-optimized triple-channel CryoProbe designed for 1H observation with 13C/15N decoupling and 13C observation with 1H decoupling due to superior sensitivity on 13C.
  • CryoProbe includes cryogenically cooled preamplifiers for 1H, 19F, 13C, 15N, and 2H
  • 19F nuclei can also be observed through the 1H channel for 19F-tagged proteins or small molecules with the highest possible sensitivity
  • A powerful technique for determining the 3D structures of proteins, nucleic acids, and complex structures, as well as for monitoring and characterizing intermolecular interactions. The Bruker 600 MHz NMR instrument can be utilized to study protein-protein and protein-ligand interactions to better understand their biological functions in solution.

We wish to remember and honor those who inhabited this Commonwealth before the arrival of the Europeans. Briefly occupying these lands were the Osage, Wyndott tribe, and Miami peoples. The Adena and Hopewell peoples, who are recognized by the naming of the time period in which they resided here, were here more permanently. Some of their mounds remain in the Lexington area, including at UK’s Adena Park.

In more recent years, the Cherokee occupied southeast Kentucky, the Yuchi southwest Kentucky, the Chickasaw extreme western Kentucky and the Shawnee central Kentucky including what is now the city of Lexington. The Shawnee left when colonization pushed through the Appalachian Mountains. Lower Shawnee Town ceremonial grounds are still visible in Greenup County.

We honor the first inhabitants who were here, respect their culture, and acknowledge the presence of their descendants who are here today in all walks of life including fellow pharmacists and healthcare professionals.