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Crowding, Molecular Volume and Plasticity: An Assessment Involving Crystallography, NMR and Simulations

Published: Wednesday, December 05, 2012
Last Updated: Wednesday, December 05, 2012
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It is suggested that crowding leads to compaction of protein structure and influences the functionally important plasticity of the molecule.

The discrepancy between the X-ray and NMR structures of Mycobacterium tuberculosis peptidyl-tRNA hydrolase in relation to the functionally important plasticity of the molecule led to molecular dynamics simulations. The X-ray and the NMR studies along with the simulations indicated an inverse correlation between crowding and molecular volume. A detailed comparison of proteins for which X-ray and the NMR structures appears to confirm this correlation. In consonance with the reported results of the investigations in cellular compartments and aqueous solution, the comparison indicates that the crowding results in compaction of the molecule as well as change in its shape, which could specifically involve regions of the molecule important in function. Crowding could thus influence the action of proteins through modulation of the functionally important plasticity of the molecule.

The article is published online in the Journal of Biosciences and is free to access.  

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