Using chirality to probe the conformational dynamics and assembly of intrinsically disordered amyloid proteins

Intrinsically disordered protein (IDP) conformers occupy large regions of conformational space and display relatively flat energy surfaces. Amyloid-forming IDPs, unlike natively folded proteins, have folding trajectories that frequently involve movements up shallow energy gradients prior to the “dow...

Descripción completa

Detalles Bibliográficos
Autores principales: Raskatov, Jevgenij A., Teplow, David B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5624888/
https://www.ncbi.nlm.nih.gov/pubmed/28970487
http://dx.doi.org/10.1038/s41598-017-10525-5

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5624888/
https://www.ncbi.nlm.nih.gov/pubmed/28970487
http://dx.doi.org/10.1038/s41598-017-10525-5

Ejemplares similares