Conformation and stability properties of B17: I. Analytical investigations using circular dichroism |
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Authors: | Hassan M. Khachfe David Atkinson |
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Affiliation: | Faculty of Sciences V, Lebanese University, Nabatieh, Lebanon, hassan.khachfe@liu.edu.lb. |
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Abstract: | Structural characterization of B17, the 17?% N-terminal domain of apo B, was carried out using circular dichroic (CD) spectroscopy, where secondary and tertiary structures were studied as a function of temperature and pH. Mild acidic conditions that correlate with histidine protonation invoked a change in the α-helix and random coil contents of the protein, with no apparent change in the β-sheet structural content. Specific changes in the structure of the protein that occur in response to temperature were also investigated to understand the stability and conformational changes of B17. Far- and near-UV CDs were used to probe the thermal changes in the protein. The protonation of some histidine residues was attributed to underlie the increase in the helical content of the protein. |
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