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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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Detalles Bibliográficos
Main Authors: Ohnishi, Satoshi, Shortle, David
Formato: Artigo
Idioma:Inglês
Publicado: Wiley-Blackwell 2003
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC2323921/
https://ncbi.nlm.nih.gov/pubmed/12824498
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