NMR Laboratory

The NMR Laboratory will include the latest state-of-the-art spectrometers for determining high resolution protein structures.

  • The following NMR spectrometers will be available:
  • Bruker 700 MHz NMR with cryoprobe
  • Bruker 500 MHz NMR with cryoprobe
  • Bruker 500 MHz NMR
  • Bruker Wide-Bore 300 MHz solid-state NMR for membrane proteins
  • Bruker 300 MHz AMX/ASX NMR

X-ray Crystallograpy Laboratory

The X-ray Crystallograpy Laboratory includes the latest facilities for protein X-ray crystallography.

  • R-H3BR rotating anode X-ray generator
  • R-AXIS IV image plate detector, Osmic mirror optics, X-Stream cryogenic system
  • Robotic protein crystallization facility

Protein Laboratory

The Protein Laboratory contains complete facilities for protein purification, peptide sequencing, and synthesis.

  • Applied Biosystems (Perkin Elmer) 433A peptide synthesizer
  • Applied Biosystems (Perkin Elmer) Protein Sequencer
  • Beckman Analytical Ultracentrifuge
  • Beckman Preparative Ultracentrifuges (3)
  • Typhoon 8600 variable mode laser imager (Molecular Dynamics)
  • LAS 1000 colled CCD Luminescent imager (Fuji Medical Instrumenta)
  • AKTA Explorer Air FPLC (Pharmacia Biotech)
  • Water Protein HPLC systems with diode array detectors (5)

Computational Laboratory

Peter Pulay and Lothar Schafer are both internationally recognized theoretical chemists, and their involvement in the Center provides the opportunity to use advanced computational methods to interpret and guide experimental studies of protein structure and inhibitor-protein interactions. Peter Pulay developed the powerful gradient method that is now widely used for calculating force fields, and received the Gold Medal Award from the International Academy of Quantum Sciences. Together with James Hinton, he has developed new highly accurate ab initio methods for calculating proton chemical shifts in protein structures. These methods will be used to improve the quality of solution structures determined by NMR spectroscopy. Currently, the NMR structure is determined using distance restraints obtained from NOESY cross-peak volumes, which are not very accurate. The NMR chemical shift will provide another class of restraints for the final structure determination. Lothar Schafer is known for his high-quality ab initio optimizations of peptide geometry, which have been used to refine the potentials for empirical force fields in several widely used protein molecular modeling algorithms. Powerful parallel processing computer systems are available in their laboratories for collaborative projects.

The advanced computational center includes state-of-the-art Linux parallel processing Clusters

Arkansas Statewide Mass Spectrometry Facility

Jackson Lay is the director of the UA-Fayetteville component of the core, has extensive experience in mass spectrometry, and has received a number of FDA awards. Alan Tackett, director of the UAMS component of the core, is highly experienced in the development of new mass spectrometry proteomics techniques. 

The UAF and UAMS components of the core are complementary, with UAF focusing on high resolution mass spectrometry to solve difficult problems in protein structure, and UAMS focusing on high-throughput proteomics applications.  Equipment in the core includes a Bruker Apex Ultra 9.4 T FT/MS, a Thermo LTQXL with Eksigent NanoLC, and numerous other mass spectrometry instruments listed in the separate section describing the MS Core.