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bioanalytical chemistry, small molecule synthesis, and drug-design.

Areas of InterestNew organic reactions, new aromatic halogenation methodologies, small molecule synthesis

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initiated the synthesis of novel small molecule inhibitors of ..

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of how protein synthesis occurred on an RNA molecule, ..

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  • Small Molecule Properties and Synthesis:

    (protein synthesis) ..

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    An Orthogonal and Modular Pathway for the Efficient Synthesis of Functionalized Small Molecules

  • Oncogenic Role of THOR , a Conserved Cancer/Testis …

    Small Molecules, Big Players: the National Cancer Institute's Initiative for Chemical Genetics Cancer Research

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Oncogenic Role of THOR, a Conserved Cancer/Testis Long Non-coding RNA

The basic geometry of amino acid residues is quite well determined from small-molecule crystal structures ; ). In terms of the accuracy of protein structure determinations, all of the bond lengths are invariant. Bond angles are also essentially invariant, except perhaps for , the backbone N—C—C angle (see Fig. 5). The -carbon is tetrahedral, which would give 110°, but there are indications from accurately refined protein structures (e.g., ; ) that can sometimes stretch to larger values in order to accommodate other strains in the structure.

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Sheila Hobbs DeWitt was born and raised in Gasport, NY. She received her B.A. from Cornell University in 1981. She obtained her Ph.D. in synthetic organic chemisty from Duke University in 1986, working with D. Sternbach. Following two years in process research at FMC Corporation, she joined the Medicinal Chemistry Department at Parke-Davis. In 1991, she was a founding member of the BioOrganic Group, which initiated the DIVERSOMER project. She is currently the Vice President of Technical Development for Diversomer Technologies, Inc., a start-up company formed to commercialize its DIVERSOMER system for small-molecule automated organic synthesis and combinatorial chemistry. Her primary interests are to develop and implement automation and enabling technologies for scientific discovery efforts.

Polymeric Systems for Controlled Drug Release - …

Anthony W. Czarnik was a graduate student at the University of Illinois at Urbana/Champaign with Nelson J. Leonard, an NIH postdoctoral fellow at Columbia University with Ronald Breslow, and a member of the faculty at Ohio State University for 10 years, and is currently Director of BioOrganic Chemistry at Parke-Davis Pharmaceutical Research. He serves on the Editorial Board of , on the Editorial Advisory Board of , and as an Editor of both the and the Fluorosensor WWW Database []. Dr. Czarnik holds adjunct appointments in the Departments of Chemistry at the University of Michigan, Ohio State University, the University of Toledo, and Wayne State University and has been an Eli Lilly awardee, a Fellow of the Alfred P. Sloan Foundation, and a Teacher-Scholar Fellow of the Camille and Henry Dreyfus Foundation. His current research interests include combinatorial chemistry as a tool for drug discovery, nucleic acids as targets for small molecule intervention, and fluorescent chemosensors of ion and molecule recognition.

26/10/1999 · Kathryn E

Theoretical calculations can provide a rather good understanding of these observed , distributions. The first approach is to calculate what conformations are allowed without bump of hard sphere atoms of van der Waals radius. Figure 9 is a "derivation diagram" of the allowed regions, showing which pair of atoms is responsible for each forbidden zone (from ). Four large regions symmetrical around 0°,0° are allowed for glycine. The presence of a -carbon produces a bump with the carbonyl oxygen of residue n - 1 that is a function only of and not and a bump with the NH of residue n + 1 that depends only on and not . When the resulting vertical and horizontal disallowed strips are removed from the Ramachandran plot, one is left with fairly large regions around the and the right-handed conformations and a small region of left-handed (Fig. 9). This outline fits the distribution observed in proteins (Fig. 7) fairly well, except for the rather frequent occurrence of residues in the bridge between the and regions. That bridge region becomes allowed if the C—C—N bond angle at the -carbon is increased (e.g., ), or if the grazing bump between N(i) and H(i+1) is otherwise softened. Detailed conformational energy calculations for alanine dipeptides (e.g., ; ) can reproduce the observed distribution in most respects, in spite of omission of all long-range and medium-range interactions.

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