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Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity
The response of titin to mechanical forces is a major determinant of the function of the heart. When placed under a pulling force, the unstructured regions of titin uncoil while its immunoglobulin (Ig) domains unfold and extend. Using single-molecule atomic force microscopy, we show that disulfide i...
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| Publicado no: | Nat Commun |
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| Principais autores: | , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Nature Publishing Group UK
2018
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5766482/ https://ncbi.nlm.nih.gov/pubmed/29330363 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-017-02528-7 |
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