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How does trigger factor's cellular location help it in its chaperone function?
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Trigger factor is a chaperone protein found in bacteria that assists in the proper folding of nascent polypeptides as they emerge from the ribosome during protein synthesis. Show more…
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What are molecular chaperones and heat shock proteins? Describe their functions. Would an intein-containing protein be successfully folded by trigger factor alone? Explain your answer.
The secreted bacterial protein OmpA has a precursor, ProOmpA, which has the amino-terminal signal sequence required for secretion. If purified ProOmpA is denatured with $8 \mathrm{M}$ urea and the urea is then removed (such as by running the protein solution rapidly through a gel filtration column), the protein can be translocated across isolated bacterial inner membranes in vitro. However, translocation becomes impossible if ProOmpA is first allowed to incubate for a few hours in the absence of urea. Furthermore, the capacity for translocation is maintained for an extended period if ProOmpA is first incubated in the presence of another bacterial protein called trigger factor. Describe the probable function of this factor.
What is the function of a molecular chaperone?
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