This Major Research Instrumentation award funds the acquisition of a 600 MHz 4-channel NMR instrument with a cryoprobe. The new spectrometer will be housed in the Stony Brook University NMR center and will be operated as a user run instrument on a fee for service basis. Projects supported by the new instrument span the range from chemical biology to protein folding, protein dynamics, studies of DNA structure, the characterization of novel carbon rich molecules and the design of novel polymers. The new NMR is thus an essential resource for university-wide efforts in Chemical Biology, Structural Biology, and Materials Science. Graduate students and postdoctoral fellows use the NMR during the course of their research. Thus, the spectrometer also supports the training of the next generation of researchers in modern state-of-the-art NMR methods. Furthermore, Stony Brook is exceptionally aggressive about including undergraduates in research. Participants in Project WISE, a university wide initiative designed to support and mentor undergraduate women in science utilize the NMR, amongst a range of other outreach programs. The results of these research and teaching efforts will be broadly disseminated through abstracts and peer reviewed publications, as well as by active participation of students and faculty at professional meetings.
This grant provided funds to purchase an NMR spectrometer equipped with a cryo-probe. NMR, or nuclear magnetic resonance, is a technique which exploits the magnetic properties of nuclei to determine the structure of molecules and to probe their internal motions (dynamics). NMR can be used to determine the structure of small molecules made in the chemical laboratory or isolated from natural sources. It can be used to determine the structure of large proteins and other biological macromolecules as well as polymers. An inherent problem with NMR is that it is a relatively insensitive method, requiring fairly large amounts of samples and long experiment times. This has motivated the search for improvements in experimental design and one of the major changes in the last 15 years had been the wide spread use of so called "cryo-probes". The cryoprobe maintains the sample at normal temperature, but cools the electronics used to detect the weak NMR signal to very low temperatures, thereby reducing noise and allowing a significant increase in sensitivity. This MRI funded proposal provided funds to purchase a modern NMR instrument with a cryo-probe for use in biochemical, chemical and structural biology research at Stony Brook University. The instrument supports a range of projects ranging from basic biological science and chemistry to more applied applications. Professor Raleigh uses the interment to study how proteins fold. Proteins have to fold to their correct three-dimensional structure to function, but are initially made as unfolded polypeptide chains. The process of protein folding is still mysterious and the Raleigh group focuses on characterizing the critical first steps in the folding process using NNR. Professor Seeliger’s team uses NMR to study the important role of protein motions, dynamics, in enzyme catalysis and in the control of proteins in involved in cellular signaling. Professor de Los Santos uses NMR to understand how damage to DNA affects important biological processes including DNA replication, mutagenesis and repair. Professor Sampson investigates proteins which function when bound to the cell membrane water interface. Interfacial proteins are an important class of enzymes and signaling molecules, however, characterizing the conformation of the active protein complex at the membrane interface is a major challenge in structural biology. Her team also uses NMR to study lipid metabolism. Professor Boon’s research focuses on the mechanisms of NO sensing and signal transduction. A critical step towards understanding how organisms respond to dissolved gases is to identify and characterize the biological sensors of these molecules. NMR plays a key role in these projects by defining the interactions one protein makes with its biological partners. The instrument also supports a wide range of other projects from studies of proteins involved in neurodegeneration, to investigations of complicated artificial polymers, to the design of inhibitors which target key bacterial enzymes, and studies of new materials. The instrument also plays a key role in the training of a large and diverse group of PhD and MS student and postdoctoral research fellows.
