NMR Screening Core and Solution Structure Core

Director: In-Ja Byeon, PhD

The NMR Screening and Solution Structure core is responsible for (1) assessing the structural properties of HIV proteins to determine their suitability for further structural study, (2) screening potential binding partners, provided by collaborators, for putative interactions with HIV proteins, and (3) structure determination of interacting complexes that have been identified through screening.

The NMR Screening and Solution Structure Core completes structural work on purified biological macromolecules and complexes (up to 80kDa) in aqueous solution. This material, produced by the Protein Production Core is, typically, uniformly 15N labeled or 15N/13C/D labeled, proteins and/or nucleic acids. Sample volumes are typically 250-500 μl and experiments are performed at temperatures and solution conditions suitable for ensuring structural and functional integrity of the molecules. In addition to solution NMR spectroscopy, two instruments (wide-bore 600 MHz and 800 MHz) have capabilities for solid state NMR, allowing us to perform work on membrane proteins.

The PCHPI makes use of the NMR facility of the Department of Structural Biology that occupies ~10,000 sq. ft. of specifically designed space in the basement of the BST3, where a complement of high-field spectrometers is housed. Overall, the NMR facility is extremely well equipped for all types of biomolecular NMR and currently has six five-channel Bruker AVANCE spectrometers, three operating at 600MHz (including one wide-bore magnet), one each at 700MHz, 800MHz, and 900MHz. All ultra shielded magnets are equipped with cryoprobes for increased sensitivity.