Article Abstract:
Trigger factor and DnaK protect nascent protein chains from misfolding and aggregation in E. coli cytosol. Studies show that trigger factor and DnaK improve the folding yield of proteins but delay folding process both in-vitro as well as in-vivo and this needs dynamic recruitment of additional trigger factor molecules to translating ribosomes.
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Article Abstract:
The organization of the motor protein myosin into cell division, cell motility, vesicular traffic requires precise temporal and spatial control. A novel interaction between the myosin chaperone UNC-45 and the C.elegans orthologs of carboxyl terminus of Hsc 70-interacting protein is examined.
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Article Abstract:
The Escherichia coli chaperonin GroEL and its cofactor GroES promote protein folding by sequestering nonnative polypeptides in a cage like structure. The contribution of this system to protein folding across the entire E. coli proteome is defined.
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