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Nonspecific shielding of unfavorable electrostatic intramolecular interactions in the erythropoietin native-state increase conformational stability and limit non-native aggregation

Previous equilibrium and kinetic folding studies of the glycoprotein erythropoietin indicate that sodium chloride increases the conformational stability of this therapeutically important cytokine, ostensibly by stabilizing the native-state [Banks DD, (2011) The Effect of Glycosylation on the Folding...

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Detalhes bibliográficos
Publicado no:Protein Sci
Autor principal: Banks, Douglas D
Formato: Artigo
Idioma:Inglês
Publicado em: BlackWell Publishing Ltd 2015
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC4420528/
https://ncbi.nlm.nih.gov/pubmed/25628168
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.2651
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