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Proteins are independent entities that start with spontaneous folding,
acquire native functional structures, and end by random degradation
--- this classical view of proteins may not be true.
Rather, accumulated evidence suggests that the life of proteins depends
on other players and that many proteins cannot become functional by themselves.
The cell thus provides elaborate systems to monitor,
assist, and control the behaviors of proteins and to make them function properly.
Many proteins require folding enzymes and molecular chaperones to attain their final conformations/assembly.
Newly synthesized proteins have to reach their specific sites of functions,
e.g. eukaryotic organelles and the bacterial periplasm and outer membrane.
Even after achieving native structures and reaching final destinations,
some proteins may drop out of the protein community due to stresses placed on cells including high temperature.
In such cases, molecular chaperones are called to repair the aberrant proteins.
If efforts to renature proteins fail,
the aberrant proteins are subjected to disposal by cellular degradation systems.
Aberrant proteins that have somehow escaped the cellular surveillance are prone to form aggregate
that can damage or kill cells, and may be therefore potential targets for therapeutic intervention.
This meeting features various aspects of these cellular systems
that assist proper achievement of the quality life of proteins. |
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