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Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin
Steady-state and transient conformational changes upon the thermal unfolding of ubiquitin were investigated with nonlinear IR spectroscopy of the amide I vibrations. Equilibrium temperature-dependent 2D IR spectroscopy reveals the unfolding of the β-sheet of ubiquitin through the loss of cross peaks...
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| Autores principales: | , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
National Academy of Sciences
2005
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC545570/ https://ncbi.nlm.nih.gov/pubmed/15630083 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0408646102 |
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