Forces behind N- and C-capping of peptidic helices

dc.contributor.authorMi, Tianxiong
dc.contributor.authorMattes, Lorenz
dc.contributor.authorPewklang, Thitima
dc.contributor.authorHauser, Karin
dc.contributor.authorBurgess, Kevin
dc.date.accessioned2026-02-02T08:00:17Z
dc.date.available2026-02-02T08:00:17Z
dc.date.issued2026
dc.description.abstractHelical peptides are primarily stabilized by intramolecular hydrogen bonds. Particular conformational arrangements, capping motifs, help precisely terminate helices by compensating for disruption of helical H-bonding patterns. This contribution explores if: (i) N-and C-caps are essentially the same; and, (ii) how differences impact their thermodynamic helix stabilities and folding kinetics.
dc.description.versionpublisheddeu
dc.identifier.doi10.1039/d5cc04856g
dc.identifier.ppn1965393268
dc.identifier.urihttps://kops.uni-konstanz.de/handle/123456789/76019
dc.language.isoeng
dc.rightsAttribution 3.0 Unported
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/
dc.subject.ddc540
dc.titleForces behind N- and C-capping of peptidic heliceseng
dc.typeJOURNAL_ARTICLE
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@article{Mi2026Force-76019,
  title={Forces behind N- and C-capping of peptidic helices},
  year={2026},
  doi={10.1039/d5cc04856g},
  number={9},
  volume={62},
  issn={1359-7345},
  journal={Chemical Communications},
  pages={3028--3031},
  author={Mi, Tianxiong and Mattes, Lorenz and Pewklang, Thitima and Hauser, Karin and Burgess, Kevin}
}
kops.citation.iso690MI, Tianxiong, Lorenz MATTES, Thitima PEWKLANG, Karin HAUSER, Kevin BURGESS, 2026. Forces behind N- and C-capping of peptidic helices. In: Chemical Communications. Royal Society of Chemistry (RSC). 2026, 62(9), S. 3028-3031. ISSN 1359-7345. eISSN 1364-548X. Verfügbar unter: doi: 10.1039/d5cc04856gdeu
kops.citation.iso690MI, Tianxiong, Lorenz MATTES, Thitima PEWKLANG, Karin HAUSER, Kevin BURGESS, 2026. Forces behind N- and C-capping of peptidic helices. In: Chemical Communications. Royal Society of Chemistry (RSC). 2026, 62(9), pp. 3028-3031. ISSN 1359-7345. eISSN 1364-548X. Available under: doi: 10.1039/d5cc04856geng
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