Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions

Proteins are marginally stable molecules that fluctuate between folded and unfolded states. Here, we provide a high-resolution description of unfolded states under refolding conditions for the N-terminal domain of the L9 protein (NTL9). We use a combination of time-resolved Förster resonance energy...

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Detalles Bibliográficos
Autores principales: Peran, Ivan, Holehouse, Alex S., Carrico, Isaac S., Pappu, Rohit V., Bilsel, Osman, Raleigh, Daniel P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: National Academy of Sciences 2019
Materias:
PNAS Plus
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7056937/
https://www.ncbi.nlm.nih.gov/pubmed/31167941
http://dx.doi.org/10.1073/pnas.1818206116

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7056937/
https://www.ncbi.nlm.nih.gov/pubmed/31167941
http://dx.doi.org/10.1073/pnas.1818206116

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