Abstract：
:Knowledge of folding/unfolding pathway is fundamental basis to study protein structure and stability. Human carbonic anhydrase II (HCAII) is a ∼29kDa, β-sheet dominated monomeric protein of 259 amino acid residues. In the present study, the urea-induced denaturation of HCAII was carried out which was a tri-phasic process, i.e., N (native) ↔ XI ↔ XII ↔ D (denatured) with stable intermediates XI and XII populated around 2 and 4M urea, respectively. The far-UV CD was used to characterize the intermediate states (XI and XII) for secondary structural content, near-UV CD for tertiary structure, dynamic light scattering for hydrodynamic radius and ANS fluorescence spectroscopy for the presence of exposed hydrophobic patches. Based on these experiments, we concluded that urea-induced XI state has characteristics of molten globule state while XII state bears characteristics features of pre-molten globule state. Characterization of the intermediates on the folding pathway will contribute to a deeper understanding of the structure-function relationship of HCAII. Furthermore, this system may provide an excellent model to study urea stress and the strategies adopted by the organisms to combat such a stress.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Wahiduzzaman,Dar MA,Haque MA,Idrees D,Hassan MI,Islam A,Ahmad Fdoi
10.1016/j.ijbiomac.2016.10.073subject
Has Abstractpub_date
2017-02-01 00:00:00pages
881-887eissn
0141-8130issn
1879-0003pii
S0141-8130(16)32117-1journal_volume
95pub_type
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