Chaperone-assisted translocation
نویسندگان
چکیده
منابع مشابه
Chaperone-assisted translocation of a polymer through a nanopore.
Using Langevin dynamics simulations, we investigate the dynamics of chaperone-assisted translocation of a flexible polymer through a nanopore. We find that increasing the binding energy ε between the chaperone and the chain and the chaperone concentration N(c) can greatly improve the translocation probability. Particularly, with increasing the chaperone concentration a maximum translocation pro...
متن کاملChaperone-assisted translocation of flexible polymers in three dimensions.
Polymer translocation through a nanometer-scale pore assisted by chaperones binding to the polymer is a process encountered in vivo for proteins. Studying the relevant models by computer simulations is computationally demanding. Accordingly, previous studies are either for stiff polymers in three dimensions or flexible polymers in two dimensions. Here, we study chaperone-assisted translocation ...
متن کاملChaperone-assisted degradation: multiple paths to destruction.
Molecular chaperones are well known as facilitators of protein folding and assembly. However, in recent years multiple chaperone-assisted degradation pathways have also emerged, including CAP (chaperone-assisted proteasomal degradation), CASA (chaperone-assisted selective autophagy), and CMA (chaperone-mediated autophagy). Within these pathways chaperones facilitate the sorting of non-native pr...
متن کاملChaperone-assisted pilus assembly and bacterial attachment.
Bacterial pili assembled by the chaperone-usher pathway can mediate microbial attachment, an early step in the establishment of an infection, by binding specifically to sugars present in host tissues. Recent work has begun to reveal the structural basis both of chaperone function in the biogenesis of these pili and of bacterial attachment.
متن کاملDegP Chaperone Suppresses Toxic Inner Membrane Translocation Intermediates
The periplasm of Gram-negative bacteria includes a variety of molecular chaperones that shepherd the folding and targeting of secreted proteins. A central player of this quality control network is DegP, a protease also suggested to have a chaperone function. We serendipitously discovered that production of the Bordetella pertussis autotransporter virulence protein pertactin is lethal in Escheri...
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ژورنال
عنوان ژورنال: Physical Biology
سال: 2004
ISSN: 1478-3967,1478-3975
DOI: 10.1088/1478-3967/1/2/004