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...

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Bibliografische gegevens
Gepubliceerd in:J Biol Chem
Hoofdauteurs: Chandrakesan, Muralidharan, Bhowmik, Debanjan, Sarkar, Bidyut, Abhyankar, Rajiv, Singh, Harwinder, Kallianpur, Mamata, Dandekar, Sucheta P., Madhu, Perunthiruthy K., Maiti, Sudipta, Mithu, Venus Singh
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: American Society for Biochemistry and Molecular Biology 2015
Onderwerpen:
Protein Structure and Folding
Online toegang: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
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