title: Conformation and stability properties of B17: I. Analytical investigations using circular dichroism.
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.
authors: Faculty of Sciences V, Lebanese University, Nabatieh, Lebanon, hassan.khachfe@liu.edu.lb
authors: Hassan M
authors: HM
authors: Khachfe
authors: David
authors: D
authors: Atkinson
mesh_terms: D000595:Amino Acid Sequence; D001055:Apolipoproteins B / Q000737:chemistry*; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D055550:Protein Stability; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013696:Temperature
chemical_list: D001055:Apolipoproteins B