Vol. 7, Issue 11 (2018)
Tracking urea induced unfolding-refolding of six-domain protein gelsolin by SAXS data analysis
Kunzes Dolma, Jyoti Nagar, Deb Endra Kumar Sahoo and Ashish
Is hydrophobic collapse model (HCM) is applicable to multi-domain proteins resulting from gene duplication/triplication? To probe this, we analyzed small angle X-ray scattering (SAXS) datasets on six-domain protein, gelsolin as function of increasing and decreasing urea. Kratky and Porod exponent plots and radius of gyration (RG) values indicated that with increase in urea, gelsolin transformed from globular to Gaussian-chain like to unfolded state. Upon reversal by dialysis at 4°C, profiles reversed back, except in presence of Ca2+ ions or low pH or at increased temperature. Overall, our results uphold that HCM is extendable to gelsolin if done under native conditions.
How to cite this article:
Kunzes Dolma, Jyoti Nagar, Deb Endra Kumar Sahoo, Ashish. Tracking urea induced unfolding-refolding of six-domain protein gelsolin by SAXS data analysis. Pharma Innovation 2018;7(11):05-11.