Crowding, molecular volume and plasticity: An assessment involving crystallography, NMR and simulations

Journal of biosciences

M Vijayan1¹  Umesh Varshney²  M Selvaraj¹  Rais Ahmad² 

[1] Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012$$;Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012$$

关键词: Molecular crowding;    molecular plasticity;    molecular shape;    peptidyl-tRNA hydrolase;    protein function;   

DOI  :  

来源: Indian Academy of Sciences

【 摘 要 】

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.

【 授权许可】

Unknown