Amino Acids

, Volume 46, Issue 1, pp 177–186 | Cite as

Proline-glutamate chimera’s side chain conformation directs the type of β-hairpin structure

  • Jyotirmoy Maity
  • Ulla I. M. Gerling
  • Stella Vukelić
  • Andreas Schäfer
  • Beate KokschEmail author
Original Article


Our aim was to study the impact of two proline chimeras, containing a glutamic acid side chain in cis- or trans-configuration, on secondary structure formation. We further investigated to what extent the configuration of the side chain contributes to the overall peptide conformation. We used a 10 residue peptide (IYSNPDGTWT) that forms a β-hairpin in water. The turn-forming proline was substituted with either a cis- or trans-proline-glutamic acid chimera, resulting in the peptides IYSNP cis -E DGTWT (P1_P cis-E ) and IYSNP trans -E DGTWT (P1_P trans-E ). We studied the conformation of the modified peptides by circular dichroism (CD) and NMR-spectroscopy, and SEC/static light scattering (SLS) analysis. NMR analysis reveals that the modified peptides maintain the β-hairpin conformation in aqueous solution. At 5 °C and pH 4.3, the peptide (P1_P cis-E ) was found to adopt two coexisting β-hairpin conformations (2:2 β-hairpin, and 3:5 β-hairpin). In contrast to that, the peptide (P1_P trans-E ) adopts a 2:2 β-hairpin that exists in equilibrium with a 4:4 β-hairpin conformation. The adoption of ordered β-hairpin structures for both modified peptides could be confirmed by CD spectroscopy, while SEC/SLS analysis showed a monomeric oligomerization state for all three investigated peptides. With the combination of several NMR methods, we were able to elucidate that even small alterations in the side chain conformation of the proline-glutamate chimera (cis or trans) can significantly influence the conformation of the adopted β-hairpin.


Proline chimera β-Hairpin conformation β-Turn Conformational analysis CD NMR 



Circular dichroism


High performance liquid chromatography


Fluorenylmethoxy carbonyl


Analytical ultracentrifugation


Size exclusion chromatography


Molecular dynamics








Trifluoroacetic acid




cis-Proline glutamate chimera


trans-proline glutamate chimera


Nuclear magnetic resonance


Proton nuclear magnetic resonance


Correlation spectroscopy


Total correlation spectroscopy


Nuclear Overhauser effect


Nuclear Overhauser effect spectroscopy


Rotating frame nuclear Overhauser effect spectroscopy


Solid phase peptide synthesis



The authors thank the Center for International Cooperation and the Dahlem Research School of Freie Universität Berlin for funding.

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

726_2013_1610_MOESM1_ESM.doc (1.3 mb)
Supplementary material 1 (DOC 1318 kb)


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Copyright information

© Springer-Verlag Wien 2013

Authors and Affiliations

  • Jyotirmoy Maity
    • 1
  • Ulla I. M. Gerling
    • 1
  • Stella Vukelić
    • 1
  • Andreas Schäfer
    • 2
  • Beate Koksch
    • 1
    Email author
  1. 1.Institut für Chemie und BiochemieFreie Universität BerlinBerlinGermany
  2. 2.Gerätezentrum BioSupraMolFreie Universität BerlinBerlinGermany

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