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Effects of denaturants and substitutions of hydrophobic residues on backbone dynamics of denatured staphylococcal nuclease
Analysis of residual dipolar couplings (RDCs) in the Δ131Δ fragment of staphylococcal nuclease has demonstrated that its ensemble-averaged structure is resistant to perturbations such as high concentrations of urea, low pH, and substitution of hydrophobic residues, suggesting that its residual struc...
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| Autors principals: | , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Wiley-Blackwell
2003
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2323921/ https://ncbi.nlm.nih.gov/pubmed/12824498 |
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