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Can I read NMR-Solution Structures in Methanol of an α-Heptapeptide, of a β3/β2-Nonapeptide, and of an all-β3-Icosapeptide Carrying the 20 Proteinogenic Side Chains on EtoBox?
NMR-Solution Structures in Methanol of an α-Heptapeptide, of a β3/β2-Nonapeptide, and of an all-β3-Icosapeptide Carrying the 20 Proteinogenic Side Chains by Dieter Seebach; Raveendra I. Mathad; Thierry Kimmerlin; Yogesh R. Mahajan; Pascal Bindschädler; Magnus Rueping; Bernhard Jaun; Christian Hilty; Touraj Etezady-Esfarjani is a Chemistry article available to read on EtoBox.
What is NMR-Solution Structures in Methanol of an α-Heptapeptide, of a β3/β2-Nonapeptide, and of an all-β3-Icosapeptide Carrying the 20 Proteinogenic Side Chains about?
## Abstract The NMR‐solution structure of an __α__‐heptapeptide with a central Aib residue was investigated in order to verify that, in contrast to __β__‐peptides, short __α__‐peptides do not form a helical structures in MeOH. Although the central Aib residue was found to induce a bend in the experimentally determined structure, no secondary structure typical for longer __α__‐peptides or proteins was found. A __β__^2^/__β__^3^‐nonapeptide with polar, positively charged side chains was subjected to NMR analysis in MeOH and H~2~O. Whereas, in MeOH, it folds into a __10/12__‐helix very similar to the structure determined for a corresponding __β__^2^/__β__^3^‐nonapeptide with only aliphatic side chains, no dominant conformation could be determined in H~2~O. Finally, the NMR analysis of a __β__^3^‐icosapeptide containing the side chains of all 20 proteinogenic amino acids in MeOH is described. It revealed that this 20mer folds into a __3__~14~‐helix over its whole length forming six full turns, the longest __3__~14~‐helix found so far. Together, our findings confirm that, in contrast to __α__‐peptides, __β__‐peptides not only form helices with just six residues, but also form helices th
Who reads NMR-Solution Structures in Methanol of an α-Heptapeptide, of a β3/β2-Nonapeptide, and of an all-β3-Icosapeptide Carrying the 20 Proteinogenic Side Chains?
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- Author
- Dieter Seebach; Raveendra I. Mathad; Thierry Kimmerlin; Yogesh R. Mahajan; Pascal Bindschädler; Magnus Rueping; Bernhard Jaun; Christian Hilty; Touraj Etezady-Esfarjani
- Publisher
- John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0018-019X)
- Published
- 2005
- Language
- EN
- Field
- Chemistry (Physical Sciences)