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Ernest Wenkert

Bio: Ernest Wenkert is an academic researcher from Indiana University. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & Carbon-13. The author has an hindex of 29, co-authored 137 publications receiving 3649 citations. Previous affiliations of Ernest Wenkert include University of California, San Diego.


Papers
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TL;DR: In this article, the reactions of alkenyl sulphides, benzenethiols, and aryl sulphides with methylmagnesium, mediated by bis(triphenylphosphine)nickel dichloride, in benzene solution have been shown to lead to olefins (predominantly with retention of configuration), toluenes, and biphenyls in medium to high yields.
Abstract: The reactions of alkenyl sulphides, benzenethiols, and aryl sulphides with methylmagnesium and arylmagnesium bromides, mediated by bis(triphenylphosphine)nickel dichloride, in benzene solution have been shown to lead to olefins (predominantly with retention of configuration), toluenes, and biphenyls in medium to high yields.

166 citations


Cited by
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TL;DR: This Review provides an overview of C-H bond functionalization strategies for the rapid synthesis of biologically active compounds such as natural products and pharmaceutical targets.
Abstract: The direct functionalization of C-H bonds in organic compounds has recently emerged as a powerful and ideal method for the formation of carbon-carbon and carbon-heteroatom bonds. This Review provides an overview of C-H bond functionalization strategies for the rapid synthesis of biologically active compounds such as natural products and pharmaceutical targets.

2,391 citations

Journal ArticleDOI
TL;DR: The use of novel two-dimensional nuclear magnetic resonance (NMR) pulse sequences to provide insight into protein dynamics is described, suggesting that there is no correlation between these rapid small amplitude motions and secondary structure for S. Nase.
Abstract: This paper describes the use of novel two-dimensional nuclear magnetic resonance (NMR) pulse sequences to provide insight into protein dynamics. The sequences developed permit the measurement of the relaxation properties of individual nuclei in macromolecules, thereby providing a powerful experimental approach to the study of local protein mobility. For isotopically labeled macromolecules, the sequences enable measurements of heteronuclear nuclear Overhauser effects (NOE) and spin-lattice (T1) and spin-spin (T2) 15N or 13C relaxation times with a sensitivity similar to those of many homonuclear 1H experiments. Because T1 values and heteronuclear NOEs are sensitive to high-frequency motions (10(8)-10(12) s-1) while T2 values are also a function of much slower processes, it is possible to explore dynamic events occurring over a large time scale. We have applied these techniques to investigate the backbone dynamics of the protein staphylococcal nuclease (S. Nase) complexed with thymidine 3',5'-bisphosphate (pdTp) and Ca2+ and labeled uniformly with 15N. T1, T2, and NOE values were obtained for over 100 assigned backbone amide nitrogens in the protein. Values of the order parameter (S), characterizing the extent of rapid 1H-15N bond motions, have been determined. These results suggest that there is no correlation between these rapid small amplitude motions and secondary structure for S. Nase. In contrast, 15N line widths suggest a possible correlation between secondary structure and motions on the millisecond time scale. In particular, the loop region between residues 42 and 56 appears to be considerably more flexible on this slow time scale than the rest of the protein.

1,760 citations