منابع مشابه
Nucleation 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 کاملMechanisms and rates of nucleation of amyloid fibrils.
The classical nucleation theory finds the rate of nucleation proportional to the monomer concentration raised to the power, which is the "critical nucleus size," nc. The implicit assumption, that amyloids nucleate in the same way, has been recently challenged by an alternative two-step mechanism, when the soluble monomers first form a metastable aggregate (micelle) and then undergo conversion i...
متن کاملAmyloid Fibrils from Hemoglobin
Amyloid fibrils are a class of insoluble protein nanofibers that are formed via the self-assembly of a wide range of peptides and proteins. They are increasingly exploited for a broad range of applications in bionanotechnology, such as biosensing and drug delivery, as nanowires, hydrogels, and thin films. Amyloid fibrils have been prepared from many proteins, but there has been no definitive ch...
متن کاملLysophospholipids induce the nucleation and extension of beta2-microglobulin-related amyloid fibrils at a neutral pH.
BACKGROUND In beta(2)-microglobulin-related (Abeta2M) amyloidosis, partial unfolding of beta(2)-microglobulin (beta2-m) is believed to be prerequisite to its assembly into Abeta2M amyloid fibrils in vivo. Low concentrations of sodium dodecyl sulfate induce partial unfolding of beta2-m to an amyloidogenic conformer and subsequent amyloid fibril formation in vitro, but the biological molecules th...
متن کاملCatalytic Nucleation of Amyloid Beta and Hen Egg White Fibrils, and p53 Oligomerization
Scaling theory generates transferable (even universal) algebraic and geometrical relations between the amino acid sequences and the aggregation functions of the three titled radically different proteins. In addition to the two hydropathicity scales and β strand scales used in earlier p53 work, a second β strand Hot Spot scale is shown to yield very accurate results for oligomerization of p53, t...
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ژورنال
عنوان ژورنال: The Journal of Chemical Physics
سال: 2010
ISSN: 0021-9606,1089-7690
DOI: 10.1063/1.3447891