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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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Detalhes bibliográficos
Main Authors: Ohnishi, Satoshi, Shortle, David
Formato: Artigo
Idioma:Inglês
Publicado em: Wiley-Blackwell 2003
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2323921/
https://ncbi.nlm.nih.gov/pubmed/12824498
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