The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness

Controlling the helical structure of peptide foldamers requires detailed understanding of the relationship between primary and secondary structure. Here the effect of monomer stoichiometry and configuration on the helical structures of peptide nucleic acids bearing sulfono pendants is examined.

Guardado en:
Detalles Bibliográficos
Autores principales: Peng Teng, Mengmeng Zheng, Darrell Cole Cerrato, Yan Shi, Mi Zhou, Songyi Xue, Wei Jiang, Lukasz Wojtas, Li-June Ming, Yong Hu, Jianfeng Cai
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
Acceso en línea:https://doaj.org/article/d9b8f9ae63dc4df88e675993e45d2ab2
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:d9b8f9ae63dc4df88e675993e45d2ab2
record_format dspace
spelling oai:doaj.org-article:d9b8f9ae63dc4df88e675993e45d2ab22021-12-02T16:57:12ZThe folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness10.1038/s42004-021-00496-02399-3669https://doaj.org/article/d9b8f9ae63dc4df88e675993e45d2ab22021-05-01T00:00:00Zhttps://doi.org/10.1038/s42004-021-00496-0https://doaj.org/toc/2399-3669Controlling the helical structure of peptide foldamers requires detailed understanding of the relationship between primary and secondary structure. Here the effect of monomer stoichiometry and configuration on the helical structures of peptide nucleic acids bearing sulfono pendants is examined.Peng TengMengmeng ZhengDarrell Cole CerratoYan ShiMi ZhouSongyi XueWei JiangLukasz WojtasLi-June MingYong HuJianfeng CaiNature PortfolioarticleChemistryQD1-999ENCommunications Chemistry, Vol 4, Iss 1, Pp 1-9 (2021)
institution DOAJ
collection DOAJ
language EN
topic Chemistry
QD1-999
spellingShingle Chemistry
QD1-999
Peng Teng
Mengmeng Zheng
Darrell Cole Cerrato
Yan Shi
Mi Zhou
Songyi Xue
Wei Jiang
Lukasz Wojtas
Li-June Ming
Yong Hu
Jianfeng Cai
The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness
description Controlling the helical structure of peptide foldamers requires detailed understanding of the relationship between primary and secondary structure. Here the effect of monomer stoichiometry and configuration on the helical structures of peptide nucleic acids bearing sulfono pendants is examined.
format article
author Peng Teng
Mengmeng Zheng
Darrell Cole Cerrato
Yan Shi
Mi Zhou
Songyi Xue
Wei Jiang
Lukasz Wojtas
Li-June Ming
Yong Hu
Jianfeng Cai
author_facet Peng Teng
Mengmeng Zheng
Darrell Cole Cerrato
Yan Shi
Mi Zhou
Songyi Xue
Wei Jiang
Lukasz Wojtas
Li-June Ming
Yong Hu
Jianfeng Cai
author_sort Peng Teng
title The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness
title_short The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness
title_full The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness
title_fullStr The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness
title_full_unstemmed The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness
title_sort folding propensity of α/sulfono-γ-aa peptidic foldamers with both left- and right-handedness
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/d9b8f9ae63dc4df88e675993e45d2ab2
work_keys_str_mv AT pengteng thefoldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT mengmengzheng thefoldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT darrellcolecerrato thefoldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT yanshi thefoldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT mizhou thefoldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT songyixue thefoldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT weijiang thefoldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT lukaszwojtas thefoldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT lijuneming thefoldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT yonghu thefoldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT jianfengcai thefoldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT pengteng foldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT mengmengzheng foldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT darrellcolecerrato foldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT yanshi foldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT mizhou foldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT songyixue foldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT weijiang foldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT lukaszwojtas foldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT lijuneming foldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT yonghu foldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
AT jianfengcai foldingpropensityofasulfonogaapeptidicfoldamerswithbothleftandrighthandedness
_version_ 1718382593148190720