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Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues

p13suc1 has two native states, a monomer and a domain-swapped dimer. We show that their folding pathways are connected by the denatured state, which introduces a kinetic barrier between monomer and dimer under native conditions. The barrier is lowered under conditions that speed up unfolding, thereb...

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Detalhes bibliográficos
Main Authors: Rousseau, F., Schymkowitz, J. W. H., Wilkinson, H. R., Itzhaki, L. S.
Formato: Artigo
Idioma:Inglês
Publicado em: The National Academy of Sciences 2001
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC33258/
https://ncbi.nlm.nih.gov/pubmed/11344301
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.101542098
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