Macromolecular crowding decelerates aggregation of a {beta}-rich protein, bovine carbonic anhydrase: a case study

In this study, we investigated the effect of synthetic macromolecular crowders on bovine carbonic anhydrase (BCA, a β-rich protein) aggregation. In contrast to the effect of macromolecular crowding on α-rich proteins, BCA aggregation was observed to be reduced due to decrease in the population of aggregation-prone intermediates as a consequence of increased native state stability. In addition, the extent of aggregation was found to depend on the nature of the crowder under consideration. Combining the published data on α-proteins and this study, we conclude that macromolecular crowding can have opposite consequences on protein aggregation process depending on the fold type of the protein.

Source: Journal of Biochemistry - October 27, 2014 Category: Biochemistry Authors: Mittal, S., Singh, L. R. Tags: Regular Papers Source Type: research