We used force-measuring optical tweezers to induce complete mechanical unfolding and refolding of individual Escherichia-coli ribonuclease H (RNase H) molecules. The protein unfolds in a two-state manner and refolds through an intermediate that correlates with the transient molten globule-like intermediate observed in bulk studies. This intermediate displays unusual mechanical compliance and unfolds at substantially lower forces than the native state. In a narrow range of forces, the molecule hops between the unfolded and intermediate states in real time. Occasionally, hopping was observed to stop as the molecule crossed the folding barrier directly from the intermediate, demonstrating that the intermediate is on-pathway. These studies allow us to map the energy landscape of RNase H.
Direct observation of the three-state folding of a single protein molecule / Cecconi, Ciro; Shank, Ea; Bustamante, C; Marqusee, S.. - In: SCIENCE. - ISSN 0036-8075. - 309(2005), pp. 2057-2060.
Data di pubblicazione: | 2005 |
Titolo: | Direct observation of the three-state folding of a single protein molecule |
Autore/i: | Cecconi, Ciro; Shank, Ea; Bustamante, C; Marqusee, S. |
Autore/i UNIMORE: | |
Digital Object Identifier (DOI): | http://dx.doi.org/10.1126/science.1116702 |
Rivista: | |
Volume: | 309 |
Pagina iniziale: | 2057 |
Pagina finale: | 2060 |
Codice identificativo ISI: | WOS:000232181900051 |
Codice identificativo Scopus: | 2-s2.0-25444512161 |
Codice identificativo Pubmed: | 16179479 |
Citazione: | Direct observation of the three-state folding of a single protein molecule / Cecconi, Ciro; Shank, Ea; Bustamante, C; Marqusee, S.. - In: SCIENCE. - ISSN 0036-8075. - 309(2005), pp. 2057-2060. |
Tipologia | Articolo su rivista |
File in questo prodotto:

I documenti presenti in Iris Unimore sono rilasciati con licenza Creative Commons Attribuzione - Non commerciale - Non opere derivate 3.0 Italia, salvo diversa indicazione.
In caso di violazione di copyright, contattare Supporto Iris