Douglas Tsao - Macromolecular crowding induces polypeptide compaction and decreases folding cooperativity

Version 1

      Publication Details (including relevant citation   information):

      Tsao, D. and Dokholyan, N. V., Physical Chemistry Chemical   Physics, 12:3491-3500, (2010)

      Abstract:

      A   cell's interior is comprised of macromolecules that can occupy up   to 40% of its available volume. Such crowded environments can   influence the stability of proteins and their rates of reaction.   Using discrete molecular dynamics simulations, we investigate how   both the size and number of neighboring crowding reagents affect   the thermodynamic and folding properties of structurally diverse   proteins. We find that crowding induces higher compaction of   proteins. We also find that folding becomes less cooperative with   the introduction of crowders into the system. The crowders may   induce alternative non-native protein conformations, thus   creating barriers for protein folding in highly crowded   media.

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