Hydrophobic Cooperativity as a Mechanism for Amyloid Nucleation
نویسندگان
چکیده
منابع مشابه
Bubble nucleation and cooperativity in DNA melting.
Bubbles in DNA are related to fundamental processes such as duplication and transcription. Using a new ensemble technique to trap intermediate states, we present direct measurements of the average length of the denaturation bubble and the statistical weights of the bubble states in the temperature-driven melting of DNA oligomers. For a bubble flanked by double-stranded regions, we find a nuclea...
متن کاملNucleation of amyloid fibrils.
We consider nucleation of amyloid fibrils in the case when the process occurs by the mechanism of direct polymerization of practically fully extended protein segments, i.e., beta-strands, into beta-sheets. Applying the classical nucleation theory, we derive a general expression for the work to form a nanosized amyloid fibril (protofilament) constituted of successively layered beta-sheets. Analy...
متن کاملReal-time monitoring of hydrophobic aggregation reveals a critical role of cooperativity in hydrophobic effect
The hydrophobic interaction drives nonpolar solutes to aggregate in aqueous solution, and hence plays a critical role in many fundamental processes in nature. An important property intrinsic to hydrophobic interaction is its cooperative nature, which is originated from the collective motions of water hydrogen bond networks surrounding hydrophobic solutes. This property is widely believed to enh...
متن کاملNanoscale hydrophobic interaction and nanobubble nucleation.
We report large-scale atomistic simulation of midrange nanoscale hydrophobic interaction, manifested by the nucleation of nanobubble between nanometer-sized hydrophobes at constrained equilibrium. When the length scale of the hydrophobes is greater than 2 nm, the nanobubble formation shows hysteresis behavior resembling the first-order transition. Calculation of the potential of mean force vers...
متن کاملProliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism.
The generation of toxic oligomers during the aggregation of the amyloid-β (Aβ) peptide Aβ42 into amyloid fibrils and plaques has emerged as a central feature of the onset and progression of Alzheimer's disease, but the molecular pathways that control pathological aggregation have proved challenging to identify. Here, we use a combination of kinetic studies, selective radiolabeling experiments, ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Molecular Biology
سال: 2007
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2007.02.043