Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein
Force-dependent transitions can provide insights into the free-energy landscape of proteins. Here, the authors observe the folding and unfolding dynamics of the model protein Csp using magnetic tweezers, from which a free-energy landscape with two energy barriers and a transient intermediate state i...
Guardado en:
Autores principales: | , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/ebd0c07ae42e46769d108bf1a5dca73b |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:ebd0c07ae42e46769d108bf1a5dca73b |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:ebd0c07ae42e46769d108bf1a5dca73b2021-11-14T12:07:21ZTwo energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein10.1038/s42004-021-00592-12399-3669https://doaj.org/article/ebd0c07ae42e46769d108bf1a5dca73b2021-11-01T00:00:00Zhttps://doi.org/10.1038/s42004-021-00592-1https://doaj.org/toc/2399-3669Force-dependent transitions can provide insights into the free-energy landscape of proteins. Here, the authors observe the folding and unfolding dynamics of the model protein Csp using magnetic tweezers, from which a free-energy landscape with two energy barriers and a transient intermediate state is constructed.Haiyan HongZilong GuoHao SunPing YuHuanhuan SuXuening MaHu ChenNature PortfolioarticleChemistryQD1-999ENCommunications Chemistry, Vol 4, Iss 1, Pp 1-7 (2021) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Chemistry QD1-999 |
spellingShingle |
Chemistry QD1-999 Haiyan Hong Zilong Guo Hao Sun Ping Yu Huanhuan Su Xuening Ma Hu Chen Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein |
description |
Force-dependent transitions can provide insights into the free-energy landscape of proteins. Here, the authors observe the folding and unfolding dynamics of the model protein Csp using magnetic tweezers, from which a free-energy landscape with two energy barriers and a transient intermediate state is constructed. |
format |
article |
author |
Haiyan Hong Zilong Guo Hao Sun Ping Yu Huanhuan Su Xuening Ma Hu Chen |
author_facet |
Haiyan Hong Zilong Guo Hao Sun Ping Yu Huanhuan Su Xuening Ma Hu Chen |
author_sort |
Haiyan Hong |
title |
Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein |
title_short |
Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein |
title_full |
Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein |
title_fullStr |
Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein |
title_full_unstemmed |
Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein |
title_sort |
two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/ebd0c07ae42e46769d108bf1a5dca73b |
work_keys_str_mv |
AT haiyanhong twoenergybarriersandatransientintermediatestatedeterminetheunfoldingandfoldingdynamicsofcoldshockprotein AT zilongguo twoenergybarriersandatransientintermediatestatedeterminetheunfoldingandfoldingdynamicsofcoldshockprotein AT haosun twoenergybarriersandatransientintermediatestatedeterminetheunfoldingandfoldingdynamicsofcoldshockprotein AT pingyu twoenergybarriersandatransientintermediatestatedeterminetheunfoldingandfoldingdynamicsofcoldshockprotein AT huanhuansu twoenergybarriersandatransientintermediatestatedeterminetheunfoldingandfoldingdynamicsofcoldshockprotein AT xueningma twoenergybarriersandatransientintermediatestatedeterminetheunfoldingandfoldingdynamicsofcoldshockprotein AT huchen twoenergybarriersandatransientintermediatestatedeterminetheunfoldingandfoldingdynamicsofcoldshockprotein |
_version_ |
1718429439859097600 |