Biology Reference
In-Depth Information
if the intrinsic structural stability of protein aggregate A, which is
reflected in the ability of this protein aggregate to fragment or be
fragmented, is higher than that of protein aggregate B, aggregate
A will grow indefinitely without generating smaller aggregates. As
a consequence, this protein aggregate will not distribute evenly
between mother and daughter cells and will be lost in contrast with
protein aggregates that remodel with ease. Finally, if the structural
characteristics of protein aggregate A allow its clearance by the
cellular degradation machinery while those of aggregate B do not,
aggregate A will propagate less efficiently than aggregate B. Thus, to
understand what makes prions “infectious” it is critical to determine
at an atomic resolution their structural characteristics and compare
them to that of protein aggregates involved in disease.
Acknowledgement
This work was supported by the CNRS and the ANR.
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