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Pathway Shifts and Thermal Softening in Temperature-Coupled Forced Unfolding of Spectrin Domains
Pathways of unfolding a protein depend in principle on the perturbation—whether it is temperature, denaturant, or even forced extension. Widely-shared, helical-bundle spectrin repeats are known to melt at temperatures as low as 40–45°C and are also known to unfold via multiple pathways as single mol...
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| Auteurs principaux: | , , , , , |
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
Biophysical Society
2003
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1303605/ https://ncbi.nlm.nih.gov/pubmed/14581229 |
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