Folding of β- and γ-peptides - the influence of substitution patterns on the formation of secondary structures

Magnus Rueping, Bernhard Jaun, Dieter Seebach

Research output: Chapter in Book/Report/Conference proceedingConference contributionpeer-review

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)]
Original languageEnglish (US)
Title of host publicationFolding of β- and γ-peptides - the influence of substitution patterns on the formation of secondary structures
Place of PublicationLaboratorium fuer Organische Chemie,Eidgenoessische Technische Hochschule,Zurich,Switz
Number of pages2
StatePublished - 2001
Externally publishedYes

Publication series

NamePeptides: The Wave of the Future, Proceedings of the Second International and the Seventeenth American Peptide Symposium, San Diego, CA, United States, June 9-14, 2001

Keywords

  • ACID
  • ACIDS
  • CONFORMATION
  • Chemical
  • Conformational Stability
  • FORM
  • NMR
  • PEPTIDE
  • PROTEIN
  • Peptides
  • Protein Folding
  • Proteins
  • SECONDARY STRUCTURE
  • SECONDARY-STRUCTURE
  • SPECTRA
  • STABILITY
  • Secondary
  • Structure
  • THERMAL-STABILITY
  • peptide folding secondary structure stability heli

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