Nucleation-dependent Aggregation Kinetics of Yeast Sup35 Fragment GNNQQNY
نویسندگان
چکیده
منابع مشابه
The Driving Forces of Peptide Aggregation: A Study of the Yeast Sup35 Prion Fragment GNNQQNY
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متن کاملA variational model for oligomer-formation process of GNNQQNY peptide from yeast prion protein Sup35.
Many human neurodegenerative diseases are associated with the aggregation of insoluble amyloid-like fibrous proteins. However, the processes by which the randomly diffused monomer peptides aggregate into the highly regulated amyloid fibril structures are largely unknown. We proposed a residue-level coarse-grained variational model for the investigation of the aggregation pathway for a small ass...
متن کاملKinetics of Amyloid Aggregation: A Study of the GNNQQNY Prion Sequence
The small amyloid-forming GNNQQNY fragment of the prion sequence has been the subject of extensive experimental and numerical studies over the last few years. Using unbiased molecular dynamics with the OPEP coarse-grained potential, we focus here on the onset of aggregation in a 20-mer system. With a total of 16.9 μs of simulations at 280 K and 300 K, we show that the GNNQQNY aggregation follow...
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The analytical characterization of biopharmaceuticals is a fundamental step in the early stages of development and prediction of their behavior in bioprocesses. Protein aggregation in particular is a common issue as it affects all stages of product development. In the present work, we investigate the stability and the aggregation kinetics of A33Fab, a therapeutically relevant humanized antibody...
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The two major forms of the amyloid-beta (Aβ) peptide found in plaques in patients suffering from Alzheimer's disease, Aβ40 and Aβ42, only differ by two amino acids in the C-terminal region, yet they display markedly different aggregation behavior. The origins of these differences have remained challenging to connect to specific molecular-level processes underlying the aggregation reaction. In t...
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ژورنال
عنوان ژورنال: Journal of Molecular Biology
سال: 2021
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2020.166732