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Functional Annotation Screening Technology by Nuclear Magnetic Resonance Spectroscopy

Kelly A Mercier, University of Nebraska - Lincoln


The past decade has brought continued success for genomics, leading to many new areas of research in chemistry, biology, and medicine. While the sequencing the genomes provides a great deal of information, the true wealth of information lies in the structure and function of these gene products. The Protein Structure Initiative was initiated in 1999 to address the need for a unified effort to address the ∼6.5 million proteins hypothesized. Since the proteins solved continually have novel folds, bioinformatics programs and databases are frequently unable to assign putative functions for these protein structures. ^ Functional Annotation Screening Technology by Nuclear Magnetic Resonance Spectroscopy was developed to assign a general biological function to proteins that lack putative function annotation. FAST-NMR is based on the premise that a biological function can be described by a similarity in binding sites and ligand interactions with proteins of known function. Using NMR techniques developed in pharmaceutical research, each protein is screened in a tierred-manner against a library of biologically active compounds. Once the functional ligands and active site are identified experimentally, the active site is then compared to all active sites in the Protein DataBase by the Comparision of Active Site Structures database and program (CPASS). The work described here encompasses the development of the FAST-NMR method, two function annotations of proteins using FAST-NMR, and a NMR structure of SR211, a Bacillus subtilis protein from the PSI. ^

Subject Area

Chemistry, Analytical|Chemistry, Nuclear

Recommended Citation

Mercier, Kelly A, "Functional Annotation Screening Technology by Nuclear Magnetic Resonance Spectroscopy" (2008). ETD collection for University of Nebraska - Lincoln. AAI3328255.