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Book Chapter

Folding of β- and γ-Peptides — the Influence of Substitution Patterns on the Formation of Secondary Structures

  • Rueping M
  • Jaun B
  • Seebach D
Springer Netherlands, (2001), 383-384
DOI: 10.1007/978-94-010-0464-0_177
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Abstract

A symposium report. The protected and unprotected b2/b3-peptides form a helix with alternating 12- and 1-membered hydrogen-bonded rings in MeOH, i.e. the both peptides adopt the same conformation in soln. g2,3,4-Hexapeptide adopts a well defined (M)-2,614-helix in soln. The stability of this helix with increasing temp. was studied by 1D-1H NMR spectra in CD3OH. [on SciFinder (R)]

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Rueping, M., Jaun, B., & Seebach, D. (2001). Folding of β- and γ-Peptides — the Influence of Substitution Patterns on the Formation of Secondary Structures. In Peptides: The Wave of the Future (pp. 383–384). Springer Netherlands. https://doi.org/10.1007/978-94-010-0464-0_177

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