D
Dieter Seebach
Researcher at ETH Zurich
Publications - 1198
Citations - 50897
Dieter Seebach is an academic researcher from ETH Zurich. The author has contributed to research in topics: Enantioselective synthesis & Amino acid. The author has an hindex of 101, co-authored 1197 publications receiving 49633 citations. Previous affiliations of Dieter Seebach include Harvard University & California Institute of Technology.
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Peptide Folding: When Simulation Meets Experiment
Xavier Daura,Karl Gademann,Bernhard Jaun,Dieter Seebach,Wilfred F. van Gunsteren,Alan E. Mark +5 more
TL;DR: Despite the small differences in sequence between the two peptides studied, the simulations correctly predict a left-handed 31-helical fold for the beta-heptapeptide and a right-handed helical Fold for thebeta-hexapeptides.
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Methods of Reactivity Umpolung
TL;DR: There are six principal methods of umpolung: 1 2n-oxidation, heteroatom exchange and modification, homologation and its reversal, the cyclopropane “trick”, use of acetylenes, and redox reactions; under certain circumstances none of these techniques is necessary in cases where direct umpoline is possible.
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The world of beta- and gamma-peptides comprised of homologated proteinogenic amino acids and other components.
TL;DR: Tests with proteolytic enzymes of all types and in vivo examination showed β‐ and γ‐peptides to be completely stable towards proteolysis and, as demonstrated for two β‐ peptides, extraordinarily stable towards metabolism, even when bearing functionalized side chains.
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Structure and Reactivity of Lithium Enolates. From Pinacolone to Selective C‐Alkylations of Peptides. Difficulties and Opportunities Afforded by Complex Structures
TL;DR: The chemistry of lithium enolates is used to demonstrate that complex structures held together by noncovalent bonds (supramolecules) may dramatically influence the result of seemingly simple standard reactions of organic synthesis as mentioned in this paper.
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β-Peptides: a surprise at every turn
TL;DR: A brief account of the results obtained since work started in this area in early 1995 is given, and the prospects for the use of β-peptides as drugs, the construction of large, enzymatically-active β-proteins and their interaction with the natural, α- peptidic counterparts are discussed.