Thomas F. Jenny
École Polytechnique Fédérale de Lausanne
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Featured researches published by Thomas F. Jenny.
Tetrahedron Letters | 1991
Thomas F. Jenny; Nicoletta Previsani; Steven A. Benner
Abstract A set of carbocyclic nucleoside analogs have been prepared using a novel modification of the Mitsunobu reaction. This approach helps solve an important synthetic problem in the preparation of carbocyclic analogs of nucleosides.
Pure and Applied Chemistry | 1998
Steven A. Benner; Thomas R. Battersby; Bernd Eschgfäller; Daniel Hutter; Janos T. Kodra; Stefan Lutz; Tuncer Arslan; D. K. Bäschlin; M. Blättler; Martin Egli; Christophe Hammer; Heike A. Held; Jennifer Horlacher; Zh. Huang; Birgitte Hyrup; Thomas F. Jenny; Simona C. Jurczyk; H. A. König; U. von Krosigk; Michael J. Lutz; L.J. MacPherson; Simon E. Moroney; E. Müller; Krishnan P. Nambiar; Joseph A. Piccirilli; C. Y. Switzer; J. J. Vögel; Clemens Richert; A. L. Roughton; Jürgen Schmidt
A research program has applied the tools of synthetic organic chemistry to systematically modify the structure of DNA and RNA oligonucleotides to learn more about the chemical principles underlying their ability to store and transmit genetic information. Oligonucleotides (as opposed to nucleosides) have long been overlooked by synthetic organic chemists as targets for structural modification. Synthetic chemistry has now yielded oligonucleotides with 12 replicatable letters, modified backbones, and new insight into why Nature chose the oligonucleotide structures that she did.
FEBS Letters | 1993
Dietlind L. Gerloff; Thomas F. Jenny; Lukas Knecht; Gaston H. Gonnet; Steven A. Benner
Surface residues, interior residues, and parsing residues, together with a secondary structure derived from these, are predicted for the MoFe nitrogenase protein in advance of a crystal structure of the protein, scheduled shortly to appear in Nature. By publishing this prediction, we test our method for predicting the conformation of proteins from patterns in the divergent evolution of homologous protein sequences in a way that places the method ‘at risk’.
Folding and Design | 1998
Gareth Chelvanayagam; Lukas Knecht; Thomas F. Jenny; Steven A. Benner; Gaston H. Gonnet
BACKGROUND Distance geometry methods allow protein structures to be constructed using a large number of distance constraints, which can be elucidated by experimental techniques such as NMR. New methods for gleaning tertiary structural information from multiple sequence alignments make it possible for distance constraints to be predicted from sequence information alone. The basic distance geometry method can thus be applied using these empirically derived distance constraints. Such an approach, which incorporates a novel combinatoric procedure, is reported here. RESULTS Given the correct sheet topology and disulfide formations, the fully automated procedure is generally able to construct native-like Calpha models for eight small beta-protein structures. When the sheet topology was unknown but disulfide connectivities were included, all sheet topologies were explored by the combinatorial procedure. Using a simple geometric evaluation scheme, models with the correct sheet topology were ranked first in four of the eight example cases, second in three examples and third in one example. If neither the sheet topology nor the disulfide connectivities were given a priori, all combinations of sheet topologies and disulfides were explored by the combinatorial procedure. The evaluation scheme ranked the correct topology within the top five folds for half the example cases. CONCLUSIONS The combinatorial procedure is a useful technique for identifying a limited number of low-resolution candidate folds for small, disulfide-rich, beta-protein structures. Better results are obtained, however, if correct disulfide connectivities are known in advance. Combinatorial distance constraints can be applied whenever there are a sufficiently small number of finite connectivities.
Tetrahedron Letters | 1992
Thomas F. Jenny; Steven A. Benne
Reaction condition are presented that allow regioselective introduction (N9 versus N7) of guanine into sugar analogs under Vorbruggen conditions. Using conditions, a set of N2-protected guanosine has been prepared with N2-isobutyryl-O6-[2-(p-nitrophenyl)ethyl]guanine (1) as nucleophile. This approach helps solve an important synthetic problem in the of guanosine analogs.
Advances in Enzyme Regulation | 1994
Steven A. Benner; Thomas F. Jenny; Mark A. Cohen; Gaston H. Gonnet
A new paradigm for predicting the secondary and tertiary structure of functional proteins from sequence data has emerged from detailed models of how natural selection, conservation, and neutral drift, the three fundamental factors in molecular evolution, leave their mark upon protein sequences. Structural information is extracted from a set of aligned homologous sequences via an analysis of patterns of conservation and variation between proteins with quantitatively defined evolutionary relationships. Tertiary structural information is obtained prior to the assignment of secondary structure, where it plays an important role. Throughout, structural predictions are made with the active involvement of a biochemist whose expertise and insight is critical both for making the prediction and in analyzing its successful and unsuccessful parts. Secondary structure predictions are evaluated based on their ability to sustain an effort to model tertiary structure. Several predictions made using the new paradigm can now be compared with those made under the classical paradigm, including a neural network. The results obtained from the new paradigm are clearly superior to those obtained with the classical paradigm, at least within the protein families that were examined.
Helvetica Chimica Acta | 1992
Thomas F. Jenny; Jennifer Horlacher; Nicoletta Previsani; Steven A. Benner
Proteins | 1995
Thomas F. Jenny; Dietlind L. Gerloff; Mark A. Cohen; Steven A. Benner
Science | 1994
Steven A. Benner; Dietlind L. Gerloff; Thomas F. Jenny
Helvetica Chimica Acta | 1993
Thomas F. Jenny