The Response of Greek Key Proteins to Changes in Connectivity Depends on the Nature of Their Secondary Structure

What governs the balance between connectivity and topology in regulating the mechanism of protein folding? We use circular permutation to vary the order of the helices in the all-α Greek key protein FADD (Fas-associated death domain) to investigate this question. Unlike all-β Greek key proteins, whe...

Descripción completa

Detalles Bibliográficos
Autores principales: Kemplen, Katherine R., De Sancho, David, Clarke, Jane
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4451459/
https://www.ncbi.nlm.nih.gov/pubmed/25861761
http://dx.doi.org/10.1016/j.jmb.2015.03.020

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4451459/
https://www.ncbi.nlm.nih.gov/pubmed/25861761
http://dx.doi.org/10.1016/j.jmb.2015.03.020

Ejemplares similares