Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/15320
Title: Equilibrium denaturation of buffalo pituitary growth hormone
Authors: Maithal, Kapil
Krishnamurty, H G
Muralidhar, K
Issue Date: Dec-2001
Publisher: NISCAIR-CSIR, India
Abstract: To understand the structural properties of buffalo growth hormone (buGH), the equilibrium denaturation using guanidinium chloride (GdmCl ) was carried out and was monitored by ultraviolet absorption spectroscopy, intrinsic fluorescence spectroscopy, far UV-circular dichroism and size-exclusion chromatography. The normalized denaturation transition curves for each of the above methods were not coincident, showing that buGH does not follow a simple two state folding mechanism. Further, size-exclusion chromatography also showed the presence of an associated intermediate during the unfolding of buGH. It was observed that in buGH, denaturation resulted in an initial disruption of the tertiary structure, whereas the secondary structure and the degree of compactness were disrupted at a higher concentration of the denaturant. This suggests that buGH follows the hierarchical model of protein folding.
Page(s): 368-374
URI: http://hdl.handle.net/123456789/15320
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.38(6) [December 2001]

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