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Single-Molecule Probes of Chaperone-Assisted Folding
W.E.
Moerner, Chemistry
Judith
Frydman, Biological Sciences
This project addresses an important biological
problem: how do proteins fold, that is, reach
their specific, native three-dimensional structures,
in the often crowded, bustling environment inside
a cell? Molecular chaperones are specialized,
barrel-shaped enzymes that accompany the newly-born
proteins until they reach their mature structure,
and prevent them from taking the “wrong
path”.
To do this, some chaperones provide a "folding
box" in which troublesome proteins may find
the necessary peace, quiet, and space to find
the proper shape required for their function.
It is not known in detail how molecular chaperones
perform their "molecular origami". In
this project, we watch what happens inside this
“folding-box”, using optical techniques
based on the emission of fluorescence from a properly-labeled
protein. While part of our measurements are based
on measuring many molecules at once, we also utilize
a relatively new method called "single-molecule
spectroscopy". In this method, lasers, microscopes,
and ultrasensitive detectors are used to follow
exactly one copy of the molecule of interest at
a time. When this is done, we can actually see
how each copy of the protein may "march to
a different drummer", which provides more
information than usual measurements that average
over many individuals. This is equivalent to watching
just one dancer on a dance floor at a time, rather
than averaging over all the dancers present which
may not be synchronized. New information on the
mechanisms of action of molecular chaperones has
been emerging from our studies.
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