Thermodynamic characterization of the conformational stability of the homodimeric protein, pea lectin

Ahmad, Nisar ; Srinivas, V. R. ; Bhanuprakash Reddy, G. ; Surolia, Avadhesha (1998) Thermodynamic characterization of the conformational stability of the homodimeric protein, pea lectin Biochemistry, 37 (47). pp. 16765-16772. ISSN 0006-2960

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Official URL: http://pubs.acs.org/doi/abs/10.1021/bi9811720

Related URL: http://dx.doi.org/10.1021/bi9811720

Abstract

The conformational stability of the homodimeric pea lectin was determined by both isothermal urea-induced and thermal denaturation in the absence and presence of urea. The denaturation profiles were analyzed to obtain the thermodynamic parameters associated with the unfolding of the protein. The data not only conform to the simple A2⇔2U model of unfolding but also are well described by the linear extrapolation model for the nature of denaturant-protein interactions. In addition, both the conformational stability (Δ Gs) and the ΔCp for the protein unfolding is quite high, at about 18.79 kcal/mol and 5.32 kcal/(mol K), respectively, which may be a reflection of the relatively larger size of the dimeric molecule (Mr 49000) and, perhaps, a consequent larger buried hydrophobic core in the folded protein. The simple two-state (A2⇔2U) nature of the unfolding process, with the absence of any monomeric intermediate, suggests that the quaternary interactions alone may contribute significantly to the conformational stability of the oligomer-a point that may be general to many oligomeric proteins.

Item Type:Article
Source:Copyright of this article belongs to American Chemical Society.
ID Code:55322
Deposited On:18 Aug 2011 12:00
Last Modified:18 Aug 2011 12:00

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