Small-angle neutron scattering studies of hemoglobin confined inside silica tubes of varying sizes

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry
Soumit S MandalAninda J Bhattacharyya

Abstract

In addition to the chemical nature of the surface, the dimensions of the confining host exert a significant influence on confined protein structures; this results in immense biological implications, especially those concerning the enzymatic activities of the protein. This study probes the structure of hemoglobin (Hb), a model protein, confined inside silica tubes with pore diameters that vary by one order of magnitude (≈20-200 nm). The effect of confinement on the protein structure is probed by comparison with the structure of the protein in solution. Small-angle neutron scattering (SANS), which provides information on protein tertiary and quaternary structures, is employed to study the influence of the tube pore diameter on the structure and configuration of the confined protein in detail. Confinement significantly influences the structural stability of Hb and the structure depends on the Si-tube pore diameter. The high radius of gyration (Rg) and polydispersity of Hb in the 20 nm diameter Si-tube indicates that Hb undergoes a significant amount of aggregation. However, for Si-tube diameters greater or equal to 100 nm, the Rg of Hb is found to be in very close proximity to that obtained from the protein data bank (PDB) reporte...Continue Reading

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Jul 25, 2012·The Journal of Physical Chemistry. B·Soumit S MandalAninda J Bhattacharyya
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Jan 29, 2013·European Biophysics Journal : EBJ·Soumit S MandalAninda J Bhattacharyya
Jun 15, 2013·Chemical Society Reviews·Martin Hartmann, Xenia Kostrov

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Citations

Jan 17, 2015·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Irina M KuznetsovaVladimir N Uversky
Jun 20, 2020·The Journal of Physical Chemistry. B·Rudra N SamajdarAninda J Bhattacharyya

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