Steric Crowding of the Turn Region Alters the Tertiary Fold of Amyloid-β(18–35) and Makes It Soluble

Aβ self-assembles into parallel cross-β fibrillar aggregates, which is associated with Alzheimer's disease pathology. A central hairpin turn around residues 23–29 is a defining characteristic of Aβ in its aggregated state. Major biophysical properties of Aβ, including this turn, remain unaltere...

Descripció completa

Guardat en:
Dades bibliogràfiques
Publicat a:J Biol Chem
Autors principals: Chandrakesan, Muralidharan, Bhowmik, Debanjan, Sarkar, Bidyut, Abhyankar, Rajiv, Singh, Harwinder, Kallianpur, Mamata, Dandekar, Sucheta P., Madhu, Perunthiruthy K., Maiti, Sudipta, Mithu, Venus Singh
Format: Artigo
Idioma:Inglês
Publicat: American Society for Biochemistry and Molecular Biology 2015
Matèries:
Protein Structure and Folding
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC4705980/
https://ncbi.nlm.nih.gov/pubmed/26487720
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M115.674135
Etiquetes: Afegir etiqueta
Sense etiquetes, Sigues el primer a etiquetar aquest registre!

Ítems similars